STRINGSTRING
hemF hemF PSHAa0088 PSHAa0088 PSHAa0089 PSHAa0089 xerC xerC PSHAa0091 PSHAa0091 PSHAa0094 PSHAa0094 cyaY cyaY PSHAa0096 PSHAa0096 PSHAa0097 PSHAa0097 hemC hemC hemDX hemDX hemY hemY cysG cysG PSHAa0546 PSHAa0546 hemA hemA PSHAa2253 PSHAa2253 hemL hemL btuR btuR cobQ cobQ hemN hemN hemE hemE hemB hemB cobU cobU cobS cobS cobT cobT PSHAa3000 PSHAa3000 PSHAb0023 PSHAb0023 hemH hemH
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
hemFCoproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX. (324 aa)
PSHAa0088Homologs of previously reported genes of unknown function. (118 aa)
PSHAa0089Putative enzyme with a phosphatase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. (234 aa)
xerCSite-specific recombinase; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. (315 aa)
PSHAa0091Conserved protein of unknown function conserved in bacteria; Homologs of previously reported genes of unknown function. (203 aa)
PSHAa0094Putative small periplasmic lipoprotein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. (64 aa)
cyaYPutative CyaY, involved in iron scavenging and/or transfer to heme; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. (107 aa)
PSHAa0096Putative phospholipase/carboxylesterase family protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. (223 aa)
PSHAa0097Homologs of previously reported genes of unknown function. (301 aa)
hemCHydroxymethylbilane synthase (porphobilinogen deaminase); Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. (312 aa)
hemDXuroporphyrinogen-III synthase HemD (N terminal)/Uroporphyrin-III C-methyltransferase (C terminal); Function of strongly homologous gene; enzyme. (616 aa)
hemYPutative HemY (Uncharacterized enzyme of heme biosynthesis); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. (368 aa)
cysGMultifunctional siroheme synthase: uroporphyrinogen methyltransferase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. (473 aa)
PSHAa0546Putative cobalamin biosynthesis protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. (314 aa)
hemAGlutamyl tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (421 aa)
PSHAa2253Putative membrane protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; membrane component. (144 aa)
hemLGlutamate-1-semialdehyde 2,1-aminomutase (GSA) (Glutamate-1-semialdehyde aminotransferase); Function of homologous gene experimentally demonstrated in an other organism; enzyme. (426 aa)
btuRcob(I)alamin and cobinamide ATP-dependent adenolsyltransferase; Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids. (199 aa)
cobQCobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. (492 aa)
hemNCoproporphyrinogen III oxidase, O2-independent, SAM and NAD(P)H dependent; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (457 aa)
hemEUroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (354 aa)
hemB5-aminolevulinate dehydratase (porphobilinogen synthase); Function of strongly homologous gene; enzyme; Belongs to the ALAD family. (336 aa)
cobUBifunctional adenosylcobalamin biosynthesis protein cobU [Includes: Adenosylcobinamide kinase; Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate. (175 aa)
cobSCobalamin 5'-phosphate synthase; Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate; Belongs to the CobS family. (274 aa)
cobTNicotinate-nucleotide dimethylbenzimidazole-P phophoribosyl transferase; Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). (353 aa)
PSHAa3000Putative enzymatic protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. (204 aa)
PSHAb0023Putative membrane protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; membrane component. (505 aa)
hemHFerrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. (339 aa)
Your Current Organism:
Pseudoalteromonas haloplanktis
NCBI taxonomy Id: 326442
Other names: P. haloplanktis TAC125, Pseudoalteromonas haloplanktis TAC125, Pseudoalteromonas haloplanktis str. TAC125, Pseudoalteromonas haloplanktis strain TAC125
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.