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
//