COBQ_SALPK
ID COBQ_SALPK Reviewed; 506 AA.
AC B5BG57;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=SSPA0797;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(2009).
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; FM200053; CAR58938.1; -; Genomic_DNA.
DR RefSeq; WP_000189676.1; NC_011147.1.
DR AlphaFoldDB; B5BG57; -.
DR SMR; B5BG57; -.
DR KEGG; sek:SSPA0797; -.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; DVRMNPL; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001869; 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_1000090248"
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
