ID F8ACJ7_THEID Unreviewed; 478 AA.
AC F8ACJ7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=Thein_0823 {ECO:0000313|EMBL:AEH44701.1};
OS Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812).
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfatatoraceae; Thermodesulfatator.
OX NCBI_TaxID=667014 {ECO:0000313|EMBL:AEH44701.1, ECO:0000313|Proteomes:UP000006793};
RN [1] {ECO:0000313|Proteomes:UP000006793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC {ECO:0000313|Proteomes:UP000006793};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders L.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermodesulfatator indicus DSM 15286.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEH44701.1, ECO:0000313|Proteomes:UP000006793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC {ECO:0000313|Proteomes:UP000006793};
RX PubMed=22768359; DOI=10.4056/sigs.2665915;
RA Anderson I., Saunders E., Lapidus A., Nolan M., Lucas S., Tice H.,
RA Del Rio T.G., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Chang Y.J.,
RA Brambilla E.M., Rohde M., Spring S., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of the thermophilic sulfate-reducing ocean
RT bacterium Thermodesulfatator indicus type strain (CIR29812(T)).";
RL Stand. Genomic Sci. 6:155-164(2012).
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}.
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DR EMBL; CP002683; AEH44701.1; -; Genomic_DNA.
DR RefSeq; WP_013907445.1; NC_015681.1.
DR AlphaFoldDB; F8ACJ7; -.
DR STRING; 667014.Thein_0823; -.
DR PaxDb; 667014-Thein_0823; -.
DR KEGG; tid:Thein_0823; -.
DR PATRIC; fig|667014.3.peg.846; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_0; -.
DR InParanoid; F8ACJ7; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000006793; Chromosome.
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:UP000006793}.
FT DOMAIN 6..225
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 253..424
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 417
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 478 AA; 53660 MW; 7C49804A61D11D03 CRC64;
MTAKVLAVLG TMSSVGKSLL TAIISYHFAK KGLKVSPFKA QNMSLNAFAT TEGEMAYAQV
FQAWAAGRKP SVKMNPLLLK PLGNMTSEII FLGKTQGILP SGKFQKFKAG FKKQVFSVFE
DILAENDLVV IEGAGGLAEL NLLKNDFVNY EIVSRYQIPF LLVGDIDRGG IFAQIWGTYE
LVPELKPLSV GFAINKFRGA PELFEDGIKI LEHKTQKPCL GLLPFLTLKL FEEDSASLGL
PNQKFSSGPE KLKIAVVYYP HISNYLDFDP LKFEPDVEVI LTAEPQELLK AHVIILPGSK
NTMASLNFLR EKGLSETIKS LSRQKILIGL CGGFQILGQK ISDEGVENLG EVPGLALLPH
ETRFFRPKIA TAQEITLNWP FFQGNLKGFE IRYGRSFLGG QEISHLFKEN IFGSYLHGIF
YEDDFRHAFL SYVRDLFGFE PRPKTFFHEF VQQQITKICK DYAFKRFLSR LEKALFIP
//
