SDHD_CITK8
ID SDHD_CITK8 Reviewed; 442 AA.
AC A8ACI7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=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=CKO_00021;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Monomer. {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; CP000822; ABV11200.1; -; Genomic_DNA.
DR RefSeq; WP_012000781.1; NC_009792.1.
DR AlphaFoldDB; A8ACI7; -.
DR SMR; A8ACI7; -.
DR STRING; 290338.CKO_00021; -.
DR EnsemblBacteria; ABV11200; ABV11200; CKO_00021.
DR GeneID; 45134330; -.
DR KEGG; cko:CKO_00021; -.
DR HOGENOM; CLU_035707_0_0_6; -.
DR OMA; ESDPNCF; -.
DR OrthoDB; 912282at2; -.
DR Proteomes; UP000008148; 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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
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.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..442
FT /note="D-serine dehydratase"
FT /id="PRO_1000063710"
FT MOD_RES 118
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 442 AA; 47767 MW; D90B217048AD9BF9 CRC64;
MENAKMTSLI AQYPLVEDLI ALKETTWFNP GTTSLAEGLP YVGLTAQDVQ DAHARLARFA
PYLAKAFPET AATGGIIESE LAIIPAMQQR LEKEYGQKIS GELLLKKDSH LPISGSIKAR
GGIYEVLAHA EKLALEAGLL TTEDDYSVML SPEFRQFFSQ YSIAVGSTGN LGLSIGIMSA
CIGFKVTVHM SADARAWKKA KLRSHGVTVV EYEEDYGVAV EQGRKAAQSD PNCFFIDDEN
SRTLFLGYAV AGQRLKAQFA QQGRVVDADH PLFVYLPCGV GGGPGGVAFG LKLAFGDNVH
CFFAEPTHSP CMLLGVYTGL HDAISVQEIG VDNLTAADGL AVGRASGFVG RAMERLLDGL
YTLDDRTMYD MLGWLAQEEG IRLEPSALAG MAGPQRVCRS TDYQQMHAFS AEQLNHATHL
VWATGGGMVP EEEMAQYLAK GR
