ID   A0A1I0SDZ6_9BACT        Unreviewed;       483 AA.
AC   A0A1I0SDZ6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=SAMN04488122_6767 {ECO:0000313|EMBL:SEW57390.1};
OS   Chitinophaga arvensicola.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=29529 {ECO:0000313|EMBL:SEW57390.1, ECO:0000313|Proteomes:UP000199310};
RN   [1] {ECO:0000313|EMBL:SEW57390.1, ECO:0000313|Proteomes:UP000199310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3695 {ECO:0000313|EMBL:SEW57390.1,
RC   ECO:0000313|Proteomes:UP000199310};
RA   de Groot N.N.;
RL   Submitted (OCT-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|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|HAMAP-Rule:MF_00028}.
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DR   EMBL; FOJG01000003; SEW57390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0SDZ6; -.
DR   STRING; 29529.SAMN04488122_6767; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000199310; 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}.
FT   DOMAIN          1..228
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          250..431
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        329
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   483 AA;  53082 MW;  EA18D83EA9A35896 CRC64;
     MFVGTASDVG KSVITAGFCR IFKQDGFTPA PFKAQNMSLN SYATPDGLEI GRAQAVQAEA
     AGVPAHTDMN PVLLKPTNDR NAQLVLHGKP AGNQSAWEYF MEDDKRQLFE EVKGAFNRLS
     ARFQPIVMEG AGSISELNLR AKDITNMRIA LHANAAVYLI ADIDRGGIFG SVYGTLALLP
     PEEKALIKGI IINKFRGDIR LFEGGRTLLE SLTGVPVTGV LPYFHDIHIE EEDAVSLSLK
     QKRFVAGHIN IAIVLLRHMS NFTDFNALEK DERVNIFYTD NPAEIAAADI IILPGSKNTI
     ADLLAIRNNG TAAAITEAHK RNKVVIGICG GYQMMGTEVA DPHGVEGRTG SIPGLGILPV
     RTVLTLEKIT QQRQFRYRHL PEVNEGYEIH MGDTVTEVAS PLNTFPDGTT DGYFLHERCW
     GTYLHGILDN STVVNDLLVQ CGKPTVAKEF NYRAFKEEQY NKLAAHIREH LDIPAVYKAL
     ALQ
//