COBQ_VARPS
ID COBQ_VARPS Reviewed; 479 AA.
AC C5CKN7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Vapar_2565;
OS Variovorax paradoxus (strain S110).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S110;
RX PubMed=21183664; DOI=10.1128/jb.00925-10;
RA Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA Ovchinnikova G., Goodwin L., Han C.;
RT "Complete genome sequence of the metabolically versatile plant growth-
RT promoting endophyte, Variovorax paradoxus S110.";
RL J. Bacteriol. 193:1183-1190(2011).
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; CP001635; ACS19191.1; -; Genomic_DNA.
DR RefSeq; WP_012747674.1; NC_012791.1.
DR AlphaFoldDB; C5CKN7; -.
DR STRING; 543728.Vapar_2565; -.
DR EnsemblBacteria; ACS19191; ACS19191; Vapar_2565.
DR GeneID; 45056834; -.
DR KEGG; vap:Vapar_2565; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_1_4; -.
DR OMA; DVRMNPL; -.
DR OrthoDB; 744477at2; -.
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..479
FT /note="Cobyric acid synthase"
FT /id="PRO_1000201973"
FT DOMAIN 250..442
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 434
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 479 AA; 50922 MW; A4580F9A66C0CBC0 CRC64;
MTTRCVMVLG TTSGAGKSWL TAALCRWYAR QGLKVAPFKA QNMSNNARVV GGGEIGSAQY
FQALAARAVP DVRMNPLLLK PERDTHSQVV LMGQVSAELT AMPWRGRSER VWPQIAQALD
ALRAENDVVV IEGAGSPAEI NLMASDIVNL RVARHADARC LLVTDIDRGG AFAHLYGTWA
LMPESDRALL RGFVLNKFRG DASLLAPAPQ QLQALTGIAT VATLPMWREH GLPEEDGVFD
DRSHASGAVT RTVAVVAYPR ISNLDEFQPL KNVPGVRLAW ARTPAELAGA DWIVLPGSKH
TSGDLAWLRA QGLDRAIAAH AARGGAVLGV CGGLQMLGEA LVDPHGIDGN APGLGLLPLV
TVFEREKTVR HRAAVFGQLG GAWASLSNVP VAGYEIHHGQ TAIHPQMAQD GHAVMPEGLA
WQNARGNVLG LYLHGLFEDA AALHALFGAA APTLDATFDG LADFIDNHFE AGVLQGLIA
