ID   A0A1M6ABE4_9VIBR        Unreviewed;       473 AA.
AC   A0A1M6ABE4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN   ECO:0000313|EMBL:SHI33688.1};
GN   ORFNames=VA7868_03531 {ECO:0000313|EMBL:SHI33688.1};
OS   Vibrio aerogenes CECT 7868.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1216006 {ECO:0000313|EMBL:SHI33688.1, ECO:0000313|Proteomes:UP000184608};
RN   [1] {ECO:0000313|EMBL:SHI33688.1, ECO:0000313|Proteomes:UP000184608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7868 {ECO:0000313|EMBL:SHI33688.1,
RC   ECO:0000313|Proteomes:UP000184608};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00025166, ECO:0000256|HAMAP-Rule:MF_00028}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00028}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00006205, ECO:0000256|HAMAP-Rule:MF_00028}.
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DR   EMBL; FQXZ01000039; SHI33688.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6ABE4; -.
DR   STRING; 1216006.VA7868_03531; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000184608; Unassembled WGS sequence.
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-UniRule.
DR   CDD; cd05389; CobQ_N; 1.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047045; CobQ_N.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00313; cobQ; 1.
DR   PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00028};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184608}.
FT   DOMAIN          8..233
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          254..406
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        333
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        444
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   473 AA;  51637 MW;  DC06C36FE483BF9E CRC64;
     MIKTSKALMV QGTTSDAGKS VLVAGLCRVL ARKGVTVAPF KPQNMALNSA VTVDGGEIGR
     AQAVQAHACG IEPTTDMNPV LLKPNTDIGA QIIIHGKALE DMDAVTYHAF KPQVMQYVIE
     SFDRLKSQYQ SVMIEGAGSP AEINLREHDI ANMGFAEAAD VPVIIVADID RGGVFAHLYG
     TLALLSESEQ SRVIGFVINR FRGDIKLLEN GLDWLEEKTG KPVIGALPYL HGLMLEAEDA
     INISQLSNDE PQLKVVVPVL QRISNHTDFD PLRMHPNVDL VFVGQHQPLP PADLIILPGS
     KSVRSDLAFL REQGWDKQIE RHLRFGGKLM GICGGYQMLG LRVADPLGLE GQAGESAGLG
     YLPLETALQA TKQLKQTHGT LSLPGQKTVD VFGYEIHAGI TQGGLRKCAA FPEWRERRSD
     WNGRAGVWQL SAWYFRVTGR MSCHSALGWI TGGARRRFCA NARRRHQPGG RCD
//