ID   COBQ_SALPA              Reviewed;         506 AA.
AC   Q5PDU3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=SPA0852;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(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}.
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DR   EMBL; CP000026; AAV76840.1; -; Genomic_DNA.
DR   RefSeq; WP_000189676.1; NC_006511.1.
DR   AlphaFoldDB; Q5PDU3; -.
DR   SMR; Q5PDU3; -.
DR   EnsemblBacteria; AAV76840; AAV76840; SPA0852.
DR   KEGG; spt:SPA0852; -.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; DVRMNPL; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000008185; 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; 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; 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..506
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002377"
FT   DOMAIN          251..448
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        440
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   506 AA;  54981 MW;  2B5FD717AC87850F CRC64;
     MTQAVMLQGT ASDVGKSVLV AGLCRIFYQD GLRTAPFKSQ NMALNSGITP DGKEMGRAQI
     FQAEAAGITP DVRMNPVLLK PTSDRQAQVV LMGKVATNMD AVSYHDYKPR LREQILAVYN
     SLAQEYDVIV LEGAGSPAEI NLRDRDIVNM GMAEMAQCPV ILVADIDRGG VFAAIYGTLA
     LLHKQERDRV KGVIINKFRG DVALLYSGIE QIESLTGVPV LGVMPWLDVD LEDEDGVALQ
     NDKYRGNAPR DITIAIVQLP HISNFTDFNA LAAQPDVRIR YIRRPEALTD ADLVILPGSK
     NTLSDLAWLR ESGMADAVLQ THRQGVPVMG ICGGYQMLGD TIVDEVESGL GTQPGLGLLN
     TITRFAQDKT TTQVNATMSG ELPGWLAAAA GLPVRGYEIH MGETVLQEGC CTAMTLQKNG
     CSVADGAVTA DGLAFGTYLH GLFDSDAFTR AVVNGLRARK GLAPWETTFC YAEHKARQFD
     LLAEAMRQHI DIDKIYTIMQ QHQEPV