ID   A0A1G8XU86_9GAMM        Unreviewed;       484 AA.
AC   A0A1G8XU86;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   ORFNames=SAMN04487954_109152 {ECO:0000313|EMBL:SDJ94111.1};
OS   Halomonas gudaonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=376427 {ECO:0000313|EMBL:SDJ94111.1, ECO:0000313|Proteomes:UP000198525};
RN   [1] {ECO:0000313|EMBL:SDJ94111.1, ECO:0000313|Proteomes:UP000198525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6133 {ECO:0000313|EMBL:SDJ94111.1,
RC   ECO:0000313|Proteomes:UP000198525};
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|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; FNES01000009; SDJ94111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8XU86; -.
DR   STRING; 376427.SAMN04487954_109152; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000198525; 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:UP000198525}.
FT   DOMAIN          1..225
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          246..433
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        325
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   484 AA;  51683 MW;  482E18648DBB4C3E CRC64;
     MIQGTTSDAG KSTVVAALCR ALARHGVSVA PFKPQNMALN SAVTADGGEI GRSTALQALA
     CGVEPHSDMN PVLLKPESDR GAQVILRGRV HGHMDALDYH AYKRQARAGV MAAWEALSSR
     YDMIIAEGAG SPAEINLRDN DIANMGFAER VDCPVLLVGD IDRGGVFAQL VGTLELLSAS
     ERARTRGFII NRFRGDLALL DPGLTWLAER TGKPVLGTLP YLDGLLLDAE DSIGRAGHDD
     GEPALRVVVP ALPRISNHND FDPLRLHPRV ALTFVGPNQV IPPSDLIVLP GSKSTRTDLA
     WLRSQGWEAA IRRHLRYGGR VLGICGGFQM LGRVVHDPEG LEGPAGSTPG LGLLDLETRM
     VPGKQLRNVA GRLSPEGVPV SGYEIHNGVS EGPALARPLV ALDDREGERA DGAVSDDGQV
     MGTYLHGLFD RPEACTALLA RCGSAAAEAA VDYREHRQRE LDRLADTVES CLDFTAIERL
     LSDG
//