STRINGSTRING
ctaB ctaB hemB hemB hemL1 hemL1 hemL2 hemL2 cysG1 cysG1 ctaA ctaA cysG2 cysG2 rutF rutF hemN hemN hemF hemF cobT1 cobT1 cobV cobV cobD cobD cobC cobC cobB cobB cobA cobA cobE cobE cobO cobO cobN cobN cobP cobP cobQ cobQ AFL53576.1 AFL53576.1 cobT2 cobT2 cobS cobS hemH hemH gltX gltX cobM cobM cobL cobL cobK cobK cobJ cobJ cobI cobI cobH cobH cobG cobG cobF cobF hemA1 hemA1 hemC hemC AFL54110.1 AFL54110.1 hemA2 hemA2 bfr bfr AFL54369.1 AFL54369.1 hemE hemE
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:
ctaBProtoheme IX farnesyltransferase CtaB; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (318 aa)
hemBDelta-aminolevulinic acid dehydratase HemB; Belongs to the ALAD family. (337 aa)
hemL1Glutamate-1-semialdehyde 2,1-aminomutase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (464 aa)
hemL2Glutamate-1-semialdehyde 2,1-aminomutase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (453 aa)
cysG1Siroheme synthase. (390 aa)
ctaAHeme A synthase CtaA; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group; Belongs to the COX15/CtaA family. Type 2 subfamily. (367 aa)
cysG2Siroheme synthase; 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. (486 aa)
rutFFMN reductase (NADH) RutF. (175 aa)
hemNOxygen-independent coproporphyrinogen-III oxidase HemN; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (450 aa)
hemFcoproporphyrinogen-III oxidase, aerobic; 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. (303 aa)
cobT1Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase CobT; Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). (338 aa)
cobVCobalamin synthase CobV; 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. (262 aa)
cobDCobalamin biosynthesis protein CobD; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. (327 aa)
cobCThreonine-phosphate decarboxylase CobC. (333 aa)
cobBCobyrinic acid A,C-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L- glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family. (431 aa)
cobAuroporphyrinogen-III C-methyltransferase CobA; Belongs to the precorrin methyltransferase family. (280 aa)
cobECobE protein CobE. (152 aa)
cobOCob(I)yrinic acid a,c-diamide adenosyltransferase; 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. (214 aa)
cobNAerobic cobaltochelatase subunit CobN. (1286 aa)
cobPBifunctional adenosylcobalamin biosynthesis protein CobP; Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate. (175 aa)
cobQCobyric acid synthase CobQ; 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. (484 aa)
AFL53576.1Cob(I)yrinic acid a,c-diamide adenosyltransferase; Belongs to the Cob(I)alamin adenosyltransferase family. (192 aa)
cobT2Aerobic cobaltochelatase subunit CobT. (631 aa)
cobSAerobic cobaltochelatase subunit CobS. (331 aa)
hemHFerrochelatase HemH; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. (358 aa)
gltXglutamate--tRNA ligase GltX; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (539 aa)
cobMPrecorrin-4 C(11)-methyltransferase CobM; Belongs to the precorrin methyltransferase family. (252 aa)
cobLprecorrin-6Y C(5,15)-methyltransferase. (413 aa)
cobKprecorrin-6A reductase CobK. (256 aa)
cobJprecorrin-3B C(17)-methyltransferase CobJ. (254 aa)
cobIPrecorrin-2 C(20)-methyltransferase CobI; Belongs to the precorrin methyltransferase family. (249 aa)
cobHprecorrin-8X methylmutase CobH. (210 aa)
cobGprecorrin-3B synthase CobG. (439 aa)
cobFprecorrin-6A synthase; Catalyzes the methylation of C-1 in precorrin-5 and the subsequent extrusion of acetic acid from the resulting intermediate to form cobalt-precorrin-6A. (256 aa)
hemA15-aminolevulinate synthase HemA. (404 aa)
hemCPorphobilinogen deaminase HemC; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. (330 aa)
AFL54110.1Putative uroporphyrinogen-III synthase protein; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. (236 aa)
hemA25-aminolevulinate synthase HemA. (429 aa)
bfrBacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. (161 aa)
AFL54369.1UPF0093 membrane protein. (179 aa)
hemEUroporphyrinogen decarboxylase HemE; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (343 aa)
Your Current Organism:
Sinorhizobium fredii USDA257
NCBI taxonomy Id: 1185652
Other names: S. fredii USDA 257, Sinorhizobium fredii USDA 257, Sinorhizobium fredii str. USDA 257, Sinorhizobium fredii strain USDA 257
Server load: low (20%) [HD]