ID   COBQ_BURMA              Reviewed;         486 AA.
AC   Q62LF1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=BMA0697;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAU49246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000010; AAU49246.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_102468.1; NC_006348.1.
DR   AlphaFoldDB; Q62LF1; -.
DR   SMR; Q62LF1; -.
DR   STRING; 243160.BMA0697; -.
DR   EnsemblBacteria; AAU49246; AAU49246; BMA0697.
DR   KEGG; bma:BMA0697; -.
DR   PATRIC; fig|243160.12.peg.718; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_4; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000006693; Chromosome 1.
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..486
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141292"
FT   DOMAIN          248..439
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   486 AA;  51224 MW;  4AA8403AA2EBF5E0 CRC64;
     MIQGTTSDAG KSTLVAGLCR LARRTGARVA PFKPQNMALN SAVTANGGEI GRAQALQALA
     AGIEAHTDLN PVLLKPTGDR GAQVIIHGTA RANLDARAYH DYKPTAMRAV LESYGRLRGA
     YDAVIVEGAG SPAEINLREG DIANMGFAEA VDCPVVLVAD IDRGGVFAHL VGTLACLSDS
     ERARVRGFVI NRFRGDPALL EPGLRWLEAR TGKPVLGVLP YLHGLTLDAE DMLPASARTS
     AARRDAGVLR IVVPALPRIS NHTDFDALRA HPRVDFTYWK RGPVPDADLL ILPGSKNVLA
     DLAWLRDAGW DALIKRHLRY GGKVIGICGG MQMLGRTLAD PHGVEGAAGA TSAGLGLLDY
     ATTLTPEKTL VNAAGRLAFG GDARVAGYEI HMGRTEGPAL ASPALMLAGR GGERPDGAVS
     ADGQILATYL HGLFDTPHAC AALLEWAGLD GAEALDYPAL REASLERLAD TFAEHLDLDR
     VFAAFA