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Database: UniProt
Entry: COBQ_MYCS2
LinkDB: COBQ_MYCS2
Original site: 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   27-MAR-2024, entry version 114.
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; Actinomycetota; Actinomycetes; Mycobacteriales; 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.MSMEG_2588; -.
DR   PaxDb; 246196-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   OrthoDB; 9808302at2; -.
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; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00313; cobQ; 1.
DR   PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
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