SDHD_CARHZ
ID SDHD_CARHZ Reviewed; 422 AA.
AC Q3AFZ5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Probable D-serine dehydratase {ECO:0000255|HAMAP-Rule:MF_01030};
DE EC=4.3.1.18 {ECO:0000255|HAMAP-Rule:MF_01030};
DE AltName: Full=D-serine deaminase {ECO:0000255|HAMAP-Rule:MF_01030};
DE Short=DSD {ECO:0000255|HAMAP-Rule:MF_01030};
GN Name=dsdA {ECO:0000255|HAMAP-Rule:MF_01030}; OrderedLocusNames=CHY_0067;
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01030};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01030};
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01030}.
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DR EMBL; CP000141; ABB15511.1; -; Genomic_DNA.
DR RefSeq; WP_011343015.1; NC_007503.1.
DR AlphaFoldDB; Q3AFZ5; -.
DR SMR; Q3AFZ5; -.
DR STRING; 246194.CHY_0067; -.
DR EnsemblBacteria; ABB15511; ABB15511; CHY_0067.
DR KEGG; chy:CHY_0067; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_9; -.
DR OMA; ESDPNCF; -.
DR OrthoDB; 912282at2; -.
DR Proteomes; UP000002706; Chromosome.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_01030; D_Ser_dehydrat; 1.
DR InterPro; IPR011780; D_Ser_am_lyase.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR48078:SF9; PTHR48078:SF9; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR02035; D_Ser_am_lyase; 1.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..422
FT /note="Probable D-serine dehydratase"
FT /id="PRO_0000291723"
FT MOD_RES 105
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 422 AA; 47309 MW; 436599EFB0D99567 CRC64;
MSDLLTGIKN YQQMFWQNPN KLSADEALAR INFSFDDIFE AQKRLQRFAP LIKKLFPETE
NGIIESPLAE IPRMKQEIEK LYGGKIHGRL FLKCDNYLKV AGSIKARGGI YEVLKHAETL
LLENGLITLE DDYSKIAEER FKKFFSNYKV AVGSTGNLGL SIGIMAAALG FKVDVHMSHD
AKEWKKKILR DRGVNVIEYR EDYSKAVEEG RKKAAAEKNT YFIDDENSRD LFLGYSVAAL
RLKDQLTELG IEVNKENPLF VYLPCGVGGA PGGISFGLKT IFKDDVYCYF VEPTHSPCML
LGLVTQKFSA IHVRDFGLDN ITEADGLAVG SPSKLVAEIA NILIDGIYTI EDEELFKLLA
LLKDSENIKV EPSAAASLKG PLLVNSRANA IHISWATGGI FIPEEIYREM YMRGKSYLKD
VY
