ID   COBQ_SHEON              Reviewed;         510 AA.
AC   Q8EI15;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=SO_1038;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN54111.1; -; Genomic_DNA.
DR   RefSeq; NP_716666.1; NC_004347.2.
DR   AlphaFoldDB; Q8EI15; -.
DR   STRING; 211586.SO_1038; -.
DR   PaxDb; Q8EI15; -.
DR   KEGG; son:SO_1038; -.
DR   PATRIC; fig|211586.12.peg.995; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   PhylomeDB; Q8EI15; -.
DR   BioCyc; SONE211586:G1GMP-961-MON; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000008186; 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..510
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141330"
FT   DOMAIN          249..458
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        336
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        450
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   510 AA;  54922 MW;  6781CC1808C3838F CRC64;
     MVQGTTSDAG KSTLVAGICR LLARQGVNVA PFKPQNMALN SAVTVDGGEI GRAQALQAAA
     CYLVPHTDFN PILLKPSSDT GAQIIVQGKA LTTLEASAFF GEKSKDYKAM ALNAVLDSFE
     RLGQQYHTIV VEGAGSPAEI NLRAGDIANM GFAEAVDCPV IIIADIDKGG VFAHLVGTLA
     LLSESEQARV KGFVINRFRG DISLLQSGID WLEAYTQKPV LGVLPYLHDL HLDAEDALTD
     SPTKQAKSCF KVRVLVYPRT SNHTDVDPLR LHPDIDFDYV SLQTQALAQT PEIAADLLIL
     PGSKNVRADL AFLREQGWDK QIAKHLRYGG KVLGICGGYQ MLGERIADPL AIEDVFGTSQ
     GLGYLPISTE FKAEKQLRCV AGELTLIGQT VAVKGYEIHC GESQYLTSSD AAKGAPLRLI
     NELTCDEQAE KSFADGCLSE DGQVLGTYLH GLFDSPDACQ LILRWAGLED AQAIDINAIR
     EQQLDRLADV LAEHLDLPQL QAILTASVKP