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COBQ_COREF
ID   COBQ_COREF              Reviewed;         493 AA.
AC   Q8FP85;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CE1900;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; BA000035; BAC18710.1; -; Genomic_DNA.
DR   RefSeq; WP_006767902.1; NZ_GG700683.1.
DR   AlphaFoldDB; Q8FP85; -.
DR   SMR; Q8FP85; -.
DR   STRING; 196164.23493741; -.
DR   EnsemblBacteria; BAC18710; BAC18710; BAC18710.
DR   KEGG; cef:CE1900; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_11; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001409; 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..493
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141300"
FT   DOMAIN          260..427
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   493 AA;  52964 MW;  10E43C75E92EE2E9 CRC64;
     MAAGPAFLIA GTTSDAGKSV ITAGLCRAFA RAGLRVAPFK AQNMSNNSAV TSDGGEIGRA
     QALQALACGL EPSVEFNPIL LKPGPDNRAR LVIRGREQGD VGAGDYIRHR HDLRGIAAAQ
     LESLRERFDI VVCEGAGSPA EINLRATDVA NFGLAQAAQL AVYIVGDIDR GGVLAHLFGT
     HAIISDEDRA LIRGFVINKF RGHQELLEPG LVQLEELTGV ETKAVIPFID DIWIDAEDSL
     QSPVGRMVGP GGRHPLGTQR LSVAAIRLPR MLGVTDVEAL AVEPGVTVTW VDDVDAVWDS
     DLVIIPGTTA TVADLAWLRH RGLDRALGER ATRGMPILGI GGGYQMMATT ITDEGDSPSS
     VAGLALFDVH IALTPHNIMV NHGDGSYEVH HGQVRHHGEQ TWIEGEGARR EALFGTHRHG
     YLQDDPARRR FLTEVATHAG KPGFLVSPDT SFHGVRLQQL DRIADVLEEH WDLDQLLDEV
     SRPANAANTP ETR
 
 
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