ID   A0A2S9I3F8_9GAMM        Unreviewed;       187 AA.
AC   A0A2S9I3F8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Cobyric acid synthase CobQ {ECO:0000313|EMBL:PRD12301.1};
DE   Flags: Fragment;
GN   ORFNames=CQW29_27295 {ECO:0000313|EMBL:PRD12301.1};
OS   Pantoea coffeiphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=1465635 {ECO:0000313|EMBL:PRD12301.1, ECO:0000313|Proteomes:UP000239181};
RN   [1] {ECO:0000313|EMBL:PRD12301.1, ECO:0000313|Proteomes:UP000239181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342 {ECO:0000313|EMBL:PRD12301.1,
RC   ECO:0000313|Proteomes:UP000239181};
RA   Siqueira K.A., Liotti R.G., Mendes T.A., Soares M.A.;
RT   "Draft genome of two endophytic bacteria isolated from 'guarana' Paullinia
RT   cupana (Mart.) Ducke.";
RL   Submitted (OCT-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}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PRD12301.1}.
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DR   EMBL; PDET01000077; PRD12301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S9I3F8; -.
DR   Proteomes; UP000239181; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
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   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR033949; CobQ_GATase1.
DR   InterPro; IPR011698; GATase_3.
DR   PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00606}.
FT   DOMAIN          60..184
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PRD12301.1"
FT   NON_TER         187
FT                   /evidence="ECO:0000313|EMBL:PRD12301.1"
SQ   SEQUENCE   187 AA;  19979 MW;  1A64829B1DD4FA9D CRC64;
     VSLLEPGLDM LKGLTGRPAY GVLPFWHGLG IDEEDGLRVS LRGAVRESAV APPLGADVLR
     VAVCAIPLMS NFTDVDALAA EPGVVVRFVD RPEELADADL VVIPGTRGTV RALRWLRERG
     LADALARRAA EHRPVLGVCG GFQILGEHIE DEVESRAGDV PGLGLLPVRV RFAREKTLTR
     PTGRALG
//