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CAJ68546.1 CAJ68546.1 hemE hemE eutT eutT CobD1 CobD1 CAJ69753.1 CAJ69753.1 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 PduX PduX cobD cobD cbiB cbiB cobB cobB cobQ cobQ cobC cobC 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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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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CAJ68546.1Putative flavodoxin. (159 aa)
hemEUroporphyrinogen decarboxylase (URO-D); Belongs to the uroporphyrinogen decarboxylase family. (340 aa)
eutTEthanolamine corrinoid cobalamin adenosyltransferase. (253 aa)
CobD1Putative threonine-phosphate decarboxylase. (358 aa)
CAJ69753.1Putative bacterioferritin; Experimentally verified through RNA-seq as part of Spo0A regulated transcriptome: down-regulated in Spo0A mutant PMID:24568651. Experimentally verified as part of mature spore proteome PMID:19542279; Belongs to the Dps family. (177 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)
PduXPutative cobalamin biosynthesis L-threonine PduX-like kinase. (295 aa)
cobDThreonine-phosphate decarboxylase (L-threonine-O-3-phosphate decarboxylase), CobD/CbiB family. (356 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)
cobCCobalamin biosynthesis phosphoglycerate mutase CobC. (204 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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