COBQ_MYCS2
ID COBQ_MYCS2 Reviewed; 496 AA.
AC A0QVI7; I7G8U3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=MSMEG_2588, MSMEI_2526;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(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; CP000480; ABK70801.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38994.1; -; Genomic_DNA.
DR RefSeq; WP_011728453.1; NZ_SIJM01000029.1.
DR RefSeq; YP_886925.1; NC_008596.1.
DR AlphaFoldDB; A0QVI7; -.
DR SMR; A0QVI7; -.
DR STRING; 246196.MSMEI_2526; -.
DR PRIDE; A0QVI7; -.
DR EnsemblBacteria; ABK70801; ABK70801; MSMEG_2588.
DR EnsemblBacteria; AFP38994; AFP38994; MSMEI_2526.
DR GeneID; 66733998; -.
DR KEGG; msg:MSMEI_2526; -.
DR KEGG; msm:MSMEG_2588; -.
DR PATRIC; fig|246196.19.peg.2554; -.
DR eggNOG; COG1492; Bacteria.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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..496
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332350"
FT DOMAIN 258..427
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 339
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 419
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 496 AA; 52179 MW; E2DCFAAF0FE4091E CRC64;
MTGGALLVAG TTSDAGKSML VGGLCRLLVR KGLSVAPFKA QNMSNNSAVT VEGGEIGRAQ
AMQARAAGLA PSVRFNPILL KPGGDRTSQL VVRGQVTGSV AAADYINHRD HLAAVVADEL
SSLREDFDAV ICEGAGSPAE INLRATDLAN MGLARAAALP VIVVGDIDRG GLLAHLHGTV
AVLEPADQAL VSGFVVNKFR GDPSLLAPGL RQLAELTGRP TYGVIPFHDE IWLDTEDSVS
VRPGGLVGAP EPPRGEQTLT VAAIRLPRIS NSTDIEALAC EPGVVVRWVT DAADLTGADL
VVIPGSKATV TDLRWLRERG LAAGIAAHAA AGRAVLGVCG GFQMLCSRID DPVESREGRV
DGLGLLDADI EFAAQKTLRH WETPLHGYEI HHGQVARSAE TDWLGIGLRR GAVYGTHWHG
LLDNDALRRD WLTEVAAAAG RDGFVVADDV DVSARRDAQL DLMADLIENH LDVGAILDLL
EHGAPHRPTM STALHV