COBQ_VIBCH
ID COBQ_VIBCH Reviewed; 484 AA.
AC Q9KLL6;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=VC_A0727;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003853; AAF96626.1; -; Genomic_DNA.
DR PIR; C82426; C82426.
DR RefSeq; NP_233114.1; NC_002506.1.
DR RefSeq; WP_000759052.1; NZ_LT906615.1.
DR AlphaFoldDB; Q9KLL6; -.
DR STRING; 243277.VC_A0727; -.
DR DNASU; 2611960; -.
DR EnsemblBacteria; AAF96626; AAF96626; VC_A0727.
DR GeneID; 57742114; -.
DR KEGG; vch:VC_A0727; -.
DR PATRIC; fig|243277.26.peg.3350; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_0_6; -.
DR OMA; GREVHDP; -.
DR BioCyc; VCHO:VCA0727-MON; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000584; Chromosome 2.
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..484
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141338"
FT DOMAIN 249..438
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 430
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 484 AA; 52575 MW; C08DEE3501B88D69 CRC64;
MKKWLMVQGT TSDAGKSVLV AGLCRVLARR GIQVCPFKPQ NMALNSAVTP DGGEIGRAQA
VQAQACGIAP SVHMNPVLLK PNSDTGAQVI LQGRALSNME ANAYHDYKKV AMDTVMDSFQ
RLQQEYEAIM IEGAGSPAEI NLRENDIANM GFAEKADVPV IIVADIDRGG VFAHLYGTLA
LLSESEQARV KGFVINRFRG DIGLLQSGLD WLEQKTGKPV IGVLPYLHGF DLEAEDAIAA
QQNLSADRQL RVAVPVFTRI SNHTDFDPLR LNPNIDFRYV GQGESLSGAD LIILPGSKST
RADLAYLRSQ GWDKEILRHL RLGGKVMGIC GGFQMLGEWV HDPLGIEGEA GSSEGLGLFA
MQTELTAEKR LTNVKGHLTL DGQTVAAQGY EIHAGHSSWA ADQKSPIILS DGSLDGLVSD
CNQGFGTYLH GIFDRPETAL RICQWAGAKE IEAYDHRAAQ ERAIDRIADA IEQHLDLTLL
WPDL