COBQ_METB6
ID COBQ_METB6 Reviewed; 480 AA.
AC A7I9K5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Mboo_1901;
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
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; CP000780; ABS56416.1; -; Genomic_DNA.
DR RefSeq; WP_012107469.1; NC_009712.1.
DR AlphaFoldDB; A7I9K5; -.
DR SMR; A7I9K5; -.
DR STRING; 456442.Mboo_1901; -.
DR EnsemblBacteria; ABS56416; ABS56416; Mboo_1901.
DR GeneID; 5410858; -.
DR KEGG; mbn:Mboo_1901; -.
DR eggNOG; arCOG00105; Archaea.
DR HOGENOM; CLU_019250_2_2_2; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 34382at2157; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002408; 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; Reference proteome.
FT CHAIN 1..480
FT /note="Probable cobyric acid synthase"
FT /id="PRO_0000332404"
FT DOMAIN 246..431
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 325
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 423
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 480 AA; 51453 MW; D07DEC69A8BEC39C CRC64;
MPLMVVGTSS HVGKSTMVAA ICRCLVRRGI RVAPFKSQNM SLNSFVTADG GEIGIAQAMQ
AWAARLSPTI DMNPVLLKPK GDCTSQVVLL GHPYKDVPIA EYYMETPYLL TEALAAYGRL
VEEYGEVVVE GAGGAAEVNL YDRDIANTLL AEKLGIPLIL VADIERGGVF AQVYGTIKLL
PAPLRPLVKG IIINKFRGDP AIFANGIRII EELTGVTVLG VVPHFSLPLP SEDSLSIGDK
RHRDLPVRIA VIRLPHISNF TDFELLEQYA AVEYVPCGGS LAGYDCIIIP GTKNTIEDLA
ALREAGTDRE ILSAREQGIP VIGICGGYQM LGATLIDDGF ESAAGEYPGL GLLDCSTRFA
TYSKNTMQVK RLAAPVSPIL VSMGEVTGYE IHMGVTDPGT DQEAFSGDGR VTADGLVFGT
YMHGLFLNPS AADALLAYLY AKKELTYSPI QTGAADPYDL LAGLFEEHVD MEAIVALLEK