Putative TonB-dependent receptor; Outer membrane TonB-dependent, hydroxamate-type ferrisiderophore receptor. Probably involved in iron transport. 30% TONB_C.IPR000531; TonB_receptor.IPR010105; TonB_siderophor. InterPro: TonB-dependent receptor protein Pfam:PF00593; TonB_dep_Rec; 1. TIGRFAMs:TIGR01783; TonB-siderophor; 1. Signal peptide present; High confidence in function and specificity.

Probable (S)-2-hydroxy-acid oxidase. Homology to gox of S. oleracea (spinach) of 42% (sprot|GOX_SPIOL). CATALYTIC ACTIVITY: (S)-2-hydroxy-acid + O(2) = 2-oxo acid + H(2)O(2). InterPro: FMN-dependent alpha-hydroxy acid dehydrogenases (IPR000262); Protein binding FMN and related compounds core region (IPR003009) Pfam: FMN-dependent dehydrogenase no signal peptide no TMHs guaA_Cterm: GMP synthase C-terminal d; Family membership.

Putative TonB-dependent receptor; Outer membrane TonB-dependent, hydroxamate-type ferrisiderophore receptor. Probably involved in iron transport. 30% TONB_C.IPR000531; TonB_receptor.IPR010105; TonB_siderophor. InterPro: TonB-dependent receptor protein Pfam:PF00593; TonB_dep_Rec; 1. TIGRFAMs:TIGR01783; TonB-siderophor; 1. Signal peptide present; High confidence in function and specificity.

Putative PKHD-type hydroxylase protein, 69% Identity(82% simialrity) to SwissProt;P59727,Q8FJM69, (48% identity) Has SMART;SM00702, P4Hc,Prolyl 4-hydroxylase alpha subunit homologues: IPR006620; Pro_4_hyd_alph; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Has PF03171,2OG-Fe(II) oxygenase superfamily;IPR005123;This family contains members of the 2-oxoglutarate [...]

Conserved hypothetical protein. Homology to TdenA01001814 of Thiobacillus denitrificans of 40% (gi|52006871|ref|ZP_00334250.1|(NBCI ENTREZ)). Has PF01402, Ribbon-helix-helix protein, copG family; IPR002145 HTH_CopG; The structure of this protein repressor, which is the shortest reported to date and the first isolated from a plasmid, has a homodimeric ribbon-helix-helix arrangement. The helix-turn-helix-like structure is involved in dimerisation and not DNA binding as might have been expected. No TMHs. No signal peptide.

Probable 1-pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.

Conserved hypothetical protein. Homology to TdenA01001814 of Thiobacillus denitrificans of 40% (gi|52006871|ref|ZP_00334250.1|(NBCI ENTREZ)). Has PF01402, Ribbon-helix-helix protein, copG family; IPR002145 HTH_CopG; The structure of this protein repressor, which is the shortest reported to date and the first isolated from a plasmid, has a homodimeric ribbon-helix-helix arrangement. The helix-turn-helix-like structure is involved in dimerisation and not DNA binding as might have been expected. No TMHs. No signal peptide.

Probable bifunctional PutA protein; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.

Conserved hypothetical protein. Homology to TdenA01001814 of Thiobacillus denitrificans of 40% (gi|52006871|ref|ZP_00334250.1|(NBCI ENTREZ)). Has PF01402, Ribbon-helix-helix protein, copG family; IPR002145 HTH_CopG; The structure of this protein repressor, which is the shortest reported to date and the first isolated from a plasmid, has a homodimeric ribbon-helix-helix arrangement. The helix-turn-helix-like structure is involved in dimerisation and not DNA binding as might have been expected. No TMHs. No signal peptide.

Putative PKHD-type hydroxylase protein, 69% Identity(82% simialrity) to SwissProt;P59727,Q8FJM69, (48% identity) Has SMART;SM00702, P4Hc,Prolyl 4-hydroxylase alpha subunit homologues: IPR006620; Pro_4_hyd_alph; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Has PF03171,2OG-Fe(II) oxygenase superfamily;IPR005123;This family contains members of the 2-oxoglutarate [...]

Putative transmembrane sensor; FecR is involved in regulation of iron dicitrate transport. In the absence of citrate FecR inactivates FecI. FecR is probably a sensor that recognizes iron dicitrate in the periplasm. Involved in iron metabolism; High confidence in function and specificity.

In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear.

Putative transmembrane sensor; FecR is involved in regulation of iron dicitrate transport. In the absence of citrate FecR inactivates FecI. FecR is probably a sensor that recognizes iron dicitrate in the periplasm. Involved in iron metabolism; High confidence in function and specificity.

Iron-regulated outer membrane protein. TonB-dependent receptor protein. Homolog to fpvA, a ferripyoverdine receptor precursor in P. aeruginosa. Similar to PupA protein of P. putida WCS,this protein is a receptor for the iron-bound form of pesudobactin, a compound structurally very; High confidence in function and specificity.

Putative transmembrane sensor; FecR is involved in regulation of iron dicitrate transport. In the absence of citrate FecR inactivates FecI. FecR is probably a sensor that recognizes iron dicitrate in the periplasm. Involved in iron metabolism; High confidence in function and specificity.

Iron-regulated outer membrane protein. TonB-dependent receptor protein. Homolog to fpvA, a ferripyoverdine receptor precursor in P. aeruginosa. Similar to PupA protein of P. putida WCS,this protein is a receptor for the iron-bound form of pesudobactin, a compound structurally very; High confidence in function and specificity.

Putative transmembrane sensor; FecR is involved in regulation of iron dicitrate transport. In the absence of citrate FecR inactivates FecI. FecR is probably a sensor that recognizes iron dicitrate in the periplasm. Involved in iron metabolism; High confidence in function and specificity.

Putative PKHD-type hydroxylase protein, 69% Identity(82% simialrity) to SwissProt;P59727,Q8FJM69, (48% identity) Has SMART;SM00702, P4Hc,Prolyl 4-hydroxylase alpha subunit homologues: IPR006620; Pro_4_hyd_alph; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Has PF03171,2OG-Fe(II) oxygenase superfamily;IPR005123;This family contains members of the 2-oxoglutarate [...]

In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear.

Putative transmembrane sensor; FecR is involved in regulation of iron dicitrate transport. In the absence of citrate FecR inactivates FecI. FecR is probably a sensor that recognizes iron dicitrate in the periplasm. Involved in iron metabolism; High confidence in function and specificity.

In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear.

Putative PKHD-type hydroxylase protein, 69% Identity(82% simialrity) to SwissProt;P59727,Q8FJM69, (48% identity) Has SMART;SM00702, P4Hc,Prolyl 4-hydroxylase alpha subunit homologues: IPR006620; Pro_4_hyd_alph; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Has PF03171,2OG-Fe(II) oxygenase superfamily;IPR005123;This family contains members of the 2-oxoglutarate [...]

In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear.

Putative PKHD-type hydroxylase protein, 69% Identity(82% simialrity) to SwissProt;P59727,Q8FJM69, (48% identity) Has SMART;SM00702, P4Hc,Prolyl 4-hydroxylase alpha subunit homologues: IPR006620; Pro_4_hyd_alph; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Has PF03171,2OG-Fe(II) oxygenase superfamily;IPR005123;This family contains members of the 2-oxoglutarate [...]

Iron-regulated outer membrane protein. TonB-dependent receptor protein. Homolog to fpvA, a ferripyoverdine receptor precursor in P. aeruginosa. Similar to PupA protein of P. putida WCS,this protein is a receptor for the iron-bound form of pesudobactin, a compound structurally very; High confidence in function and specificity.

Putative transmembrane sensor; FecR is involved in regulation of iron dicitrate transport. In the absence of citrate FecR inactivates FecI. FecR is probably a sensor that recognizes iron dicitrate in the periplasm. Involved in iron metabolism; High confidence in function and specificity.

Iron-regulated outer membrane protein. TonB-dependent receptor protein. Homolog to fpvA, a ferripyoverdine receptor precursor in P. aeruginosa. Similar to PupA protein of P. putida WCS,this protein is a receptor for the iron-bound form of pesudobactin, a compound structurally very; High confidence in function and specificity.

Putative PKHD-type hydroxylase protein, 69% Identity(82% simialrity) to SwissProt;P59727,Q8FJM69, (48% identity) Has SMART;SM00702, P4Hc,Prolyl 4-hydroxylase alpha subunit homologues: IPR006620; Pro_4_hyd_alph; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Has PF03171,2OG-Fe(II) oxygenase superfamily;IPR005123;This family contains members of the 2-oxoglutarate [...]

Iron-regulated outer membrane protein. TonB-dependent receptor protein. Homolog to fpvA, a ferripyoverdine receptor precursor in P. aeruginosa. Similar to PupA protein of P. putida WCS,this protein is a receptor for the iron-bound form of pesudobactin, a compound structurally very; High confidence in function and specificity.

Putative transmembrane sensor; FecR is involved in regulation of iron dicitrate transport. In the absence of citrate FecR inactivates FecI. FecR is probably a sensor that recognizes iron dicitrate in the periplasm. Involved in iron metabolism; High confidence in function and specificity.

Iron-regulated outer membrane protein. TonB-dependent receptor protein. Homolog to fpvA, a ferripyoverdine receptor precursor in P. aeruginosa. Similar to PupA protein of P. putida WCS,this protein is a receptor for the iron-bound form of pesudobactin, a compound structurally very; High confidence in function and specificity.

Putative PKHD-type hydroxylase protein, 69% Identity(82% simialrity) to SwissProt;P59727,Q8FJM69, (48% identity) Has SMART;SM00702, P4Hc,Prolyl 4-hydroxylase alpha subunit homologues: IPR006620; Pro_4_hyd_alph; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Has PF03171,2OG-Fe(II) oxygenase superfamily;IPR005123;This family contains members of the 2-oxoglutarate [...]

Probable (S)-2-hydroxy-acid oxidase. Homology to gox of S. oleracea (spinach) of 42% (sprot|GOX_SPIOL). CATALYTIC ACTIVITY: (S)-2-hydroxy-acid + O(2) = 2-oxo acid + H(2)O(2). InterPro: FMN-dependent alpha-hydroxy acid dehydrogenases (IPR000262); Protein binding FMN and related compounds core region (IPR003009) Pfam: FMN-dependent dehydrogenase no signal peptide no TMHs guaA_Cterm: GMP synthase C-terminal d; Family membership.

Putative TonB-dependent receptor; Outer membrane TonB-dependent, hydroxamate-type ferrisiderophore receptor. Probably involved in iron transport. 30% TONB_C.IPR000531; TonB_receptor.IPR010105; TonB_siderophor. InterPro: TonB-dependent receptor protein Pfam:PF00593; TonB_dep_Rec; 1. TIGRFAMs:TIGR01783; TonB-siderophor; 1. Signal peptide present; High confidence in function and specificity.

Probable (S)-2-hydroxy-acid oxidase. Homology to gox of S. oleracea (spinach) of 42% (sprot|GOX_SPIOL). CATALYTIC ACTIVITY: (S)-2-hydroxy-acid + O(2) = 2-oxo acid + H(2)O(2). InterPro: FMN-dependent alpha-hydroxy acid dehydrogenases (IPR000262); Protein binding FMN and related compounds core region (IPR003009) Pfam: FMN-dependent dehydrogenase no signal peptide no TMHs guaA_Cterm: GMP synthase C-terminal d; Family membership.

Putative PKHD-type hydroxylase protein, 69% Identity(82% simialrity) to SwissProt;P59727,Q8FJM69, (48% identity) Has SMART;SM00702, P4Hc,Prolyl 4-hydroxylase alpha subunit homologues: IPR006620; Pro_4_hyd_alph; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Has PF03171,2OG-Fe(II) oxygenase superfamily;IPR005123;This family contains members of the 2-oxoglutarate [...]

Probable 1-pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.

Conserved hypothetical protein. Homology to TdenA01001814 of Thiobacillus denitrificans of 40% (gi|52006871|ref|ZP_00334250.1|(NBCI ENTREZ)). Has PF01402, Ribbon-helix-helix protein, copG family; IPR002145 HTH_CopG; The structure of this protein repressor, which is the shortest reported to date and the first isolated from a plasmid, has a homodimeric ribbon-helix-helix arrangement. The helix-turn-helix-like structure is involved in dimerisation and not DNA binding as might have been expected. No TMHs. No signal peptide.

Probable 1-pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.

Probable bifunctional PutA protein; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.