COBQ_METMJ
ID COBQ_METMJ Reviewed; 492 AA.
AC A3CX25;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Memar_1999;
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
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; CP000562; ABN57925.1; -; Genomic_DNA.
DR RefSeq; WP_011844834.1; NC_009051.1.
DR AlphaFoldDB; A3CX25; -.
DR SMR; A3CX25; -.
DR STRING; 368407.Memar_1999; -.
DR EnsemblBacteria; ABN57925; ABN57925; Memar_1999.
DR GeneID; 4847714; -.
DR KEGG; mem:Memar_1999; -.
DR eggNOG; arCOG00105; Archaea.
DR HOGENOM; CLU_019250_2_2_2; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 34382at2157; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002146; 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_0000332403"
FT DOMAIN 248..434
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 327
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 426
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 492 AA; 52900 MW; 8D5DBF0806BC9D90 CRC64;
MSLIVLGTAS HVGKSMTVAA LCRALYRRGI PVAPFKSQNM SLNSYVTVDG SEIGIAQAVQ
AFAAGIEPEA DMNPILLKPK GDSVSQVVLL GRPYKDVQIR DYYRETDTLL AEAVSAFERL
RSRFGNVVVE GAGGAAEVNL YDRDIANIRL ARSLRLPIVL VADIERGGVF AQVYGTLALL
PEDIRPLVAG IIVNKFRGDP GLFAPGVAKL EELTGVPVLG VVPFADIPLP SEDSLSIADK
RDRKTGTPVR IAVVRLPRIS NFTDFELLEE HVAVDYVPPG GTLSGYDCII LPGTKNTVED
LAALNRHGVG EELRLARERG VPIIGICGGY QMLGRRIVDA GIESENPAEY AGFGLLDVVT
AFTGYRKTTV QVRRRATGPG PILPAMGEVD GYEIHMGETE RGDLSEAFAG EGASTPDGLV
FGTYMHGLFQ NPGAANALLA YLAKRRGVAF EPVTAESTAL GAAASYDDLA RHFEEHVDMD
AIMKYFIDRR SE