COBQ_METM7
ID COBQ_METM7 Reviewed; 492 AA.
AC A6VGF5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=MmarC7_0462;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
RL Submitted (JUN-2007) 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:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; CP000745; ABR65531.1; -; Genomic_DNA.
DR RefSeq; WP_011976863.1; NC_009637.1.
DR AlphaFoldDB; A6VGF5; -.
DR STRING; 426368.MmarC7_0462; -.
DR EnsemblBacteria; ABR65531; ABR65531; MmarC7_0462.
DR GeneID; 5329516; -.
DR KEGG; mmz:MmarC7_0462; -.
DR eggNOG; arCOG00105; Archaea.
DR HOGENOM; CLU_019250_2_2_2; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 34382at2157; -.
DR UniPathway; UPA00148; -.
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; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 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 PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase.
FT CHAIN 1..492
FT /note="Probable cobyric acid synthase"
FT /id="PRO_1000002365"
FT DOMAIN 252..444
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 492 AA; 54788 MW; 5E6CC8BA294B069B CRC64;
MAKFIMVVGT SSNSGKTVLV SGICRMLSNK GYKVAPFKSQ NMSLNSRVSI EDGEIAVAQY
TQAMAARAEP SVHFNPILLK PKGNFISQVI VHGTPYEDRD YNEYRSNKDD MLEKIKESID
YLDTNYDYVV IEGAGSCCEI NLLKDDIANL RIAEISGADA ILVSDIDRGG VFAAIYGTVQ
LLPENWRKLL KGFVINKFRG NIDVLKDGFE KIEELTNIPV IGTIPYDETL ILPEEDSQAL
EGKRVFGNLK SPIEVNIVKF SKIANFTDVD PLSSDCLMRY LDFNDDITGD ILILPGTRCS
TVEMDLMKKH GMDKKIMEFI ERGGIILGIC GGYQTLGKML IDENFSEGDV GTISGLGLFD
METTFGNKKA IKNSTGKISI FDQNFDVAGY ELHEGYSVSN ETPLISLSRG FGNCGNSYDG
SFKVVGNSYI FGTYFHGILE NFEFRNYLVN IVNNRKNLSK IENDNYAEIF NKNMDKLSKL
IEESLDLSKI IK