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Database: UniProt
Entry: A0A1E3G2X8_9BACT
LinkDB: A0A1E3G2X8_9BACT
Original site: A0A1E3G2X8_9BACT 
ID   A0A1E3G2X8_9BACT        Unreviewed;       275 AA.
AC   A0A1E3G2X8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=A4H02_04520 {ECO:0000313|EMBL:ODN30522.1};
OS   Fervidobacterium thailandense.
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=1008305 {ECO:0000313|EMBL:ODN30522.1, ECO:0000313|Proteomes:UP000094570};
RN   [1] {ECO:0000313|Proteomes:UP000094570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FC2004 {ECO:0000313|Proteomes:UP000094570};
RA   Gonzalez J.M., Cuecas A., Kanoksilapatham W.;
RT   "The genome sequence project of a novel Fervidobacterium isolate from a hot
RT   spring in Thailand.";
RL   Submitted (APR-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00028}.
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:ODN30522.1}.
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DR   EMBL; LWAF01000005; ODN30522.1; -; Genomic_DNA.
DR   RefSeq; WP_069292992.1; NZ_LWAF01000005.1.
DR   AlphaFoldDB; A0A1E3G2X8; -.
DR   STRING; 1008305.A4H02_04520; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000094570; 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-KW.
DR   CDD; cd05389; CobQ_N; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00028; CobQ; 1.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR047045; CobQ_N.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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          5..228
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
SQ   SEQUENCE   275 AA;  30435 MW;  990EED0434BE36DA CRC64;
     MAKTLMIVGS MSSVGKSTLV TGLCRIFSNR GYKVAPFKAQ NMSTFLTECE PGTFISTAQY
     LQALAAREKP SHLMNPIILK PLGNMRSEVY VLGKPYSVAS VGSYESLKEN LWETVKWALE
     QLLEKYDLVI IEGAGSPVEL NLKDGDIVNM RVASYVHAPT IIVGDIERGG IFAQLLGTYW
     LMTEDERQLV KGLIVNKFKG DVSLFTDGVK ILEERSGLPV LGVVPYFETN LPPEDSLSGN
     FDRPNDINDA IFDHIARTLE NHLSIGKLKS LVFEM
//
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