ID   COBQ_VIBC3              Reviewed;         484 AA.
AC   A5EZT5; C3M5K6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN   OrderedLocusNames=VC0395_0666, VC395_A0585;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACP11419.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000626; ABQ19260.1; -; Genomic_DNA.
DR   EMBL; CP001236; ACP11419.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000759054.1; NZ_JAACZH010000013.1.
DR   AlphaFoldDB; A5EZT5; -.
DR   SMR; A5EZT5; -.
DR   STRING; 345073.VC395_A0585; -.
DR   EnsemblBacteria; ABQ19260; ABQ19260; VC0395_0666.
DR   KEGG; vco:VC0395_0666; -.
DR   KEGG; vcr:VC395_A0585; -.
DR   PATRIC; fig|345073.21.peg.3326; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; GREVHDP; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000249; Chromosome 1.
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; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
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; PF01656; CbiA; 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.
FT   CHAIN           1..484
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000071011"
FT   DOMAIN          249..438
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        430
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   484 AA;  52593 MW;  F54E9833A7DE16A6 CRC64;
     MKKWLMVQGT TSDAGKSVLV AGLCRVLARR GIQVCPFKPQ NMALNSAVTP DGGEIGRAQA
     VQAQACGIAP SVHMNPVLLK PNSDTGAQVI LQGRALSNME ANAYHDYKKV AMDTVMDSFQ
     RLQQEYEAIM IEGAGSPAEI NLRENDIANM GFAEKADVPV IIVADIDRGG VFAHLYGTLA
     LLSESEQARV KGFVINRFRG DIGLLQSGLD WLEQKTGKPV IGVLPYLHGF DLEAEDAIAA
     QQNLSADRQL RVAVPVFTRI SNHTDFDPLR LNPNIDFRYV GQGESLSGAD LIILPGSKST
     RADLAYLRSQ GWDKEILRHL RLGGKVMGIC GGFQMLGEWV HDPLGIEGEA GSSEGLGLFA
     MQTELTAEKR LTNVQGHLTL DGQTVAAQGY EIHAGRSSWA ADQKSPIILS DGSLDGLVSD
     CNQGFGTYLH GIFDRPETAL RICQWAGAKE IEAYDHRAAQ ERAIDRIADA IEQHLNLTLL
     WPDL