ID   A0A1Y5SWS0_9RHOB        Unreviewed;       493 AA.
AC   A0A1Y5SWS0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:SLN46801.1};
GN   ORFNames=ROA7023_01943 {ECO:0000313|EMBL:SLN46801.1};
OS   Roseisalinus antarcticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseisalinus.
OX   NCBI_TaxID=254357 {ECO:0000313|EMBL:SLN46801.1, ECO:0000313|Proteomes:UP000193900};
RN   [1] {ECO:0000313|EMBL:SLN46801.1, ECO:0000313|Proteomes:UP000193900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7023 {ECO:0000313|EMBL:SLN46801.1,
RC   ECO:0000313|Proteomes:UP000193900};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) 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; FWFZ01000008; SLN46801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5SWS0; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000193900; 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:UP000193900}.
FT   DOMAIN          5..237
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          251..440
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        331
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   493 AA;  51194 MW;  FCB510A6841FC7A8 CRC64;
     MTKAIMIQGA GSNVGKSLLV AGLCRAVHRR GLSVAPFKPQ NMSNNAAVTA DGGEIGRAQA
     LQARAAGLAP TVDMNPVLLK PETDTGAQVI VQGRRTATLR ARDYGRMKST LLPSVLESYR
     RLAAAHDLVL VEGAGSPAEV NLRAGDIANM GFAEAAGCPV VLVGDIDRGG VIAQLVGTHV
     VLPPEDRARI KAFAINKFRG DPTLFAEGMT AIRDHTGWAG LGILPWFADA WRLPAEDVMD
     IRPKPDGGPV RIAVPRLGRI ANFDDLDPLS AEPGVSVDII EPGRPLPGDA ALVLIPGTKS
     TIADLADFRA QGWDVDLAAH VRRGGHVLGL CGGYQMLGRR IADPDGIEGP PGAVAGLGLL
     DIETTMGPVK EVTLTTATHR ASGLPVTGYE IHIGRTTGAD CARPWLDLAG RAGRAGTPEG
     ASSADGRILG CYLHGLFAAD GFRAAYLAGL GAPAAAQGFD AGVETTLDAL ARHLEAHLDV
     EALLDLASRL PAP
//