COBQ_CLOPE
ID COBQ_CLOPE Reviewed; 487 AA.
AC Q8XLJ6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CPE1045;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC and one molecule of ATP is hydrogenolyzed for each amidation.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; BA000016; BAB80751.1; -; Genomic_DNA.
DR RefSeq; WP_011010197.1; NC_003366.1.
DR AlphaFoldDB; Q8XLJ6; -.
DR SMR; Q8XLJ6; -.
DR STRING; 195102.gene:10490308; -.
DR EnsemblBacteria; BAB80751; BAB80751; BAB80751.
DR GeneID; 29571586; -.
DR KEGG; cpe:CPE1045; -.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT CHAIN 1..487
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141297"
FT DOMAIN 249..435
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 427
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 487 AA; 54632 MW; 8930BD8A5AF8510A CRC64;
MKYKSIMLLG TASSVGKSTV AAAFCRYFKK KGYRVAPYKA LNISLNSFVT KEGDEIGRAQ
VVQAEACEID PKEYMNPILM KPSAGFKTQV IVRGKVHCTM DAYKYKELNK YLKEKAKEAY
DDISNDYDLI VLEGSGSCAE INLRETDIAN MHTAKIADAD VILVADINRG GVFASIVGTI
MLLTEEERKR VKGVIINKFR GKREFFEPAM RQIEEIIKIP VLGVMPYFDL DIEEEDSASI
KLRKGNGKGI DIAIVRLPHM SNFTDFNSLG RIKDVGIRYA ENPKDLENAN MIIIPGSKNT
IDDLIYLKES GFKEALINES SNGKLIFGIC GGYQILGEKI IDSLGVEGDI REEEGLGLLN
IVTSFNKEKT TKQVVAFDLE GNEVSGYEIH NGESVPTAKE NIWIKEKNGN VLGMNNKEQN
VFGTYIHGIF DEGDFGEKLI NKLKKELNIE ESNEVNYKDY KMSQYDKLCE LLEENIDMAY
VENLIRS
