COBQ_METBU
ID COBQ_METBU Reviewed; 495 AA.
AC Q12TL2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Mbur_2361;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(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; CP000300; ABE53214.1; -; Genomic_DNA.
DR RefSeq; WP_011500349.1; NC_007955.1.
DR AlphaFoldDB; Q12TL2; -.
DR SMR; Q12TL2; -.
DR STRING; 259564.Mbur_2361; -.
DR EnsemblBacteria; ABE53214; ABE53214; Mbur_2361.
DR GeneID; 3998948; -.
DR KEGG; mbu:Mbur_2361; -.
DR HOGENOM; CLU_019250_2_2_2; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 34382at2157; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001979; 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..495
FT /note="Probable cobyric acid synthase"
FT /id="PRO_0000332402"
FT DOMAIN 256..441
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 433
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 495 AA; 53728 MW; FEE931029BCFE324 CRC64;
MTANNANKKH LLVLGTASHV GKSAIVTALC RIFSADHKVA PFKAQNMSLN SWITVDGKEI
GIAQAIQAKA AGVEPTADMN PVLLKPKGDR VSQVILLGEP YADKSAGAYY DSIEETHDVL
KGALKRLEAE YDLIVMEGAG GAAEINLYDR DIVNIGTARI TDAPIILVGD IERGGVFASL
YGTIQLLPED VRKNVRGLII NKFRGDPAIL ESGLTELEEL TGIPVLGVMP YFKLRIPSED
SVSIGDKSAD DGEHYDVDIA VIRLTRISNF TDFEPLEHMA KVRYVDLSDD LGNPDAIIIP
GTKNTTSDLN DLVESGMADK IKSFYGMVPI LGICGGYQML GKSIVDSGIE GGESARLDGL
GLLDIETVFD AYEKRTVQVT KTVKESGPIF DSIKGEDVKG YEIHMGISSS KRPVFGDDGC
ADDSGLVIGT YLHGLFDNVN IRRALISYLL EKKGLEFKEE EIPDKDPYDE LADVARENLD
MNKIYGMIGL EPEKV