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CAJ70280.1 CAJ70280.1 purC purC cbiM cbiM cbiN cbiN PurC1 PurC1 CAJ68546.1 CAJ68546.1 hemE hemE eutT eutT CAJ69092.1 CAJ69092.1 hemN hemN hemZ hemZ sirC sirC hemB hemB cobA cobA hemC hemC cbiK cbiK cbiJ cbiJ cbiH cbiH cbiG cbiG cbiF cbiF cbiT cbiT cbiE cbiE cbiD cbiD cbiC cbiC cbiB cbiB cobB cobB cobQ cobQ cobS cobS cobU cobU cobT cobT
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
CAJ70280.1Putative conjugative transposon protein Tn916-like, CTn7-Orf13. (69 aa)
purCPhosphoribosylaminoimidazole-succinocarboxamide synthase; Belongs to the SAICAR synthetase family. (232 aa)
cbiMCobalamin biosynthesis protein; Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. (250 aa)
cbiNABC-type transport system, cobalt-specific extracellular solute-binding protein; Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import; Belongs to the CbiN family. (94 aa)
PurC1Putative phosphoribosylaminoimidazole-succinocarboxamide synthetase; Experimentally verified through Mass Spectrometry as part of Spo0A regulated proteome: down-regulated in Spo0A mutant PMID:24568651. (226 aa)
CAJ68546.1Putative flavodoxin. (159 aa)
hemEUroporphyrinogen decarboxylase (URO-D); Belongs to the uroporphyrinogen decarboxylase family. (340 aa)
eutTEthanolamine corrinoid cobalamin adenosyltransferase. (253 aa)
CAJ69092.1Putative flavodoxin. (174 aa)
hemNOxygen-independent coproporphyrinogen-III oxidase (Coproporphyrinogenase) (Coprogen oxidase); Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (391 aa)
hemZCoproporphyrinogen III oxidase. (519 aa)
sirCPrecorrin-2 dehydrogenase. (192 aa)
hemBDelta-aminolevulinic acid dehydratase (porphobilinogen synthase); Belongs to the ALAD family. (321 aa)
cobABifunctional uroporphyrinogen-III methyltransferase/uroporphyrinogen-III synthase. (499 aa)
hemCPorphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. (301 aa)
cbiKSirohydrochlorin cobaltochelatase. (492 aa)
cbiJCobalt-precorrin-6A reductase. (250 aa)
cbiHCobalt-factor III methyltransferase; Cobalt-precorrin-3B C(17)-methyltransferase (Cobalt-precorrin-3 methyltransferase) (Cobalt-precorrin-3 methylase). (241 aa)
cbiGCobalamin biosynthesis protein CbiG. (373 aa)
cbiFCobalt-precorrin-4 C(11)-methyltransferase (Cobalt-precorrin-3 methylase). (250 aa)
cbiTCobalt-precorrin-6Y C(15)-methyltransferase. (191 aa)
cbiECobalt-precorrin-7 (C5)-methyl transferase; Cobalt-precorrin-6Y C(5)-methyltransferase (Cobalt-precorrin-6 methyltransferase) (Cobalt-precorrin-6Y methylase). (202 aa)
cbiDCobalt-precorrin-6A synthase [deacetylating]; Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. (408 aa)
cbiCCobalt-precorrin-8X methylmutase (Cobalt-precorrin isomerase) (HBA synthase). (210 aa)
cbiBCobalamin biosynthesis protein CbiB, CobD/CbiB family; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. (323 aa)
cobBCobyrinic acid A,C-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family. (458 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. (504 aa)
cobSCobalamin synthase CobS (Cobalamin-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. (257 aa)
cobUBifunctional adenosylcobalamin biosynthesis protein CobU [Adenosylcobinamide kinase; Adenosylcobinamide-phosphate guanylyltransferase]. (186 aa)
cobTNicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase; Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). (348 aa)
Your Current Organism:
Clostridioides difficile
NCBI taxonomy Id: 272563
Other names: C. difficile 630, Clostridioides difficile 630, Clostridium difficile 630, Clostridium difficile 630 (epidemic type X), Clostridium difficile str. 630, Clostridium difficile strain 630, Peptoclostridium difficile 630
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