ID   COBQ_XANC5              Reviewed;         478 AA.
AC   Q3BQB5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-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=XCV3317;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM039952; CAJ25048.1; -; Genomic_DNA.
DR   RefSeq; WP_011348308.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BQB5; -.
DR   STRING; 316273.XCV3317; -.
DR   EnsemblBacteria; CAJ25048; CAJ25048; XCV3317.
DR   KEGG; xcv:XCV3317; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_0_6; -.
DR   OMA; GREVHDP; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000007069; 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.
FT   CHAIN           1..478
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332401"
FT   DOMAIN          250..437
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        429
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   478 AA;  51615 MW;  F37A93F58394918A CRC64;
     MSARVLMVQG CTSDAGKSTL VAALCRWLHR QGIAVAPFKP QNMALNSAVT VDGGEIGRAQ
     ALQAQACGLE PQTDFNPVLL KPNSDTGAQV IVHGHPVATL DAVGYHAYKA TAFNAVLASH
     ARLVERFDVV LVEGAGSPAE INLRDNDIAN MGYAEAVDCA VILVADIDRG GVFAHLVGTL
     ALLSASERAR VAGVVINRFR GDLALLQPGL AWLERETGKP VLGVLPYLHG LQLDAEDAVP
     RNAPQEPQSQ LRVVVPVLPR ISNHTDVDAL LAHPQVDVRL IGPGQTPPPC DLILLPGSKS
     TRHDLQWLRT HGWDAAIARH LRYGGKLLGI CGGLQMLGTH LHDPRGIEGA AGSSPGLGWL
     SLQTTLQPHK QLHRVHGRLL LGDASVSGYE IHCALSSGAA LARPLLQLDD GRTDGAISDD
     GQVLGTYVHG VFDHPMHWLH CWRGPVWRRP RHWILPRCAK PAWSVWPMRC TRIWIPRH