COBQ_METM5
ID COBQ_METM5 Reviewed; 492 AA.
AC A4FWW2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=MmarC5_0375;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-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; CP000609; ABO34691.1; -; Genomic_DNA.
DR RefSeq; WP_011868146.1; NC_009135.1.
DR AlphaFoldDB; A4FWW2; -.
DR STRING; 402880.MmarC5_0375; -.
DR EnsemblBacteria; ABO34691; ABO34691; MmarC5_0375.
DR GeneID; 4928436; -.
DR KEGG; mmq:MmarC5_0375; -.
DR eggNOG; arCOG00105; Archaea.
DR HOGENOM; CLU_019250_2_2_2; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 34382at2157; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000253; 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-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_1000002364"
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; 54775 MW; BCA36D27DEA5BA1E CRC64;
MAKFIMVVGT SSNSGKTVLV SGICRMLSNK GYKVAPFKSQ NMSLNSRVSI EDGEIAVAQY
TQAMAARSEP SVHFNPILLK PKGNFVSQVI VHGIPYEDRD YNEYRSKKDD FLDKIKQSIN
YLDKNYDYVV IEGAGSCCEI NLLKDDIANL RVAEIAGADA ILVSDIDRGG VFASIYGTVQ
LLPENWRNLL KGFVINKFRG NIDVLKDGFE KIEELTKIPV IGTILYDETL ILPEEDSQAL
EGKRVFGNVK SPIEVNIVKF SKIANFTDVD PLSSDCLMKY IDFNDDITGD ILILPGTRCS
TVEMDLMKKH GLDKKILEFV ENGGIVLGIC GGYQTLGKML IDEDFSEGDI GTISGLGLFD
METTFGNEKA IKNSTGTISI FDQNFNVTGY ELHEGHSVSN ETPLISLSRG FGNCGDSYDG
SFKIIGNSYI FGTYFHGILE NFEFRNYLVN FVRHKKNLSK IENDNYAEIF NENMDKLSKL
VEESLDLSKI IK