ID   A0A1Y5TC32_9RHOB        Unreviewed;       484 AA.
AC   A0A1Y5TC32;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-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:SLN57046.1};
GN   ORFNames=TRL7639_03080 {ECO:0000313|EMBL:SLN57046.1};
OS   Falsiruegeria litorea R37.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Falsiruegeria.
OX   NCBI_TaxID=1200284 {ECO:0000313|EMBL:SLN57046.1, ECO:0000313|Proteomes:UP000193077};
RN   [1] {ECO:0000313|EMBL:SLN57046.1, ECO:0000313|Proteomes:UP000193077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7639 {ECO:0000313|EMBL:SLN57046.1,
RC   ECO:0000313|Proteomes:UP000193077};
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; FWFO01000002; SLN57046.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5TC32; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000193077; 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; 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; 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:UP000193077}.
FT   DOMAIN          5..237
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          249..432
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        426
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   484 AA;  51655 MW;  94AC766A3894E617 CRC64;
     MVQAIMIQGT GSNVGKSMLV AGLTRAFSRR GLRVAPFKPQ NMSNNAAVAV GGEIGRAQAL
     QARAAGLEPH TDMNPILLKP ETDTGAQIIV QGQRRGTMQA GDYRKGKAQL LAAALESFHR
     LCADADLVLL EGAGSPAETN LRAGDIANMG FACAAGVPVV LVGDIHRGGV IAQIVGTQAV
     LDDTDLAQIS GFAVNRFKGD VTLFDEGRDD IAARTGWPCL GVVPWFNDAW KLPAEDMMDI
     RSHLGGACKI VVPQLERMAN FDDLDPLSGE PNVSVEIIPA GRPLPGDADL VLLPGSKSTI
     GDLNYFRAQG WDIDLYAHVR RGGHVVGLCG GYQMLGKTIA DPEGIEGFIG EVEGLGLLDV
     HTTMAGQKKV TQTQATDIHT GLPVYGYEIH IGRTEGPDCD RPWLQVGERS EGAISPSGRV
     RGSYLHGTFA SDSYRAAFLQ ELGHRSDLSY EESVEATLDD LADHLERHMD LDLLLQLARA
     PKGL
//