COBQ_METBF
ID COBQ_METBF Reviewed; 485 AA.
AC Q466W7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Mbar_A3191;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ72075.1; -; Genomic_DNA.
DR RefSeq; WP_011308115.1; NC_007355.1.
DR AlphaFoldDB; Q466W7; -.
DR SMR; Q466W7; -.
DR STRING; 269797.Mbar_A3191; -.
DR EnsemblBacteria; AAZ72075; AAZ72075; Mbar_A3191.
DR GeneID; 3627133; -.
DR KEGG; mba:Mbar_A3191; -.
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..485
FT /note="Probable cobyric acid synthase"
FT /id="PRO_0000332405"
FT DOMAIN 250..435
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 427
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 485 AA; 53302 MW; 60C35462E1C43ADD CRC64;
MEKKSVLILG TASHVGKSSV VTAICRILSR EYRVAPFKAQ NMSLNSWITK DGKEIGIAQA
IQAKAAGTEP TADMNPVLLK PKGDCVSQII LLGEPYADRS AGKYYESIAE MNEVLEGALK
RLCNEHDIIV MEGAGGAAEI NLYERDIVNI GTARLTQAPI ILVGDIERGG VFASLYGTVA
LLPEDVRKNV KGFIINKFRG DLEILKPGLK QLEEKTGIPV LGVLPYFKLN IPSEDSVSLE
DKEAEKNEKE IEIAVIRLPR ISNFTDFEPL ERSAKIRYVE LDEDLGTPDA IMIPGTKNTV
NDLLDLKASG MAEKIQAFKG KIPIFGICGG YQMLGKTIYD SGVENGVEAE FEGLGLLDIG
TKFGEYKKRT IQVTKKVSAY GPILAPIDGE EIKGYEIHMG ITDSCRNIFG NDGAIDKAGL
VIGTYLHGLF DNKNIRDALM QYLYEKKGLE YIPENSMTES DAYEELANVV EQNLDMEKFY
EIIGI