SDHD_VIBPA
ID SDHD_VIBPA Reviewed; 443 AA.
AC Q87QA2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=VP1248;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC59511.1; -; Genomic_DNA.
DR RefSeq; NP_797627.1; NC_004603.1.
DR RefSeq; WP_005483547.1; NC_004603.1.
DR AlphaFoldDB; Q87QA2; -.
DR SMR; Q87QA2; -.
DR STRING; 223926.28806236; -.
DR EnsemblBacteria; BAC59511; BAC59511; BAC59511.
DR GeneID; 1188753; -.
DR KEGG; vpa:VP1248; -.
DR PATRIC; fig|223926.6.peg.1187; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_6; -.
DR OMA; ESDPNCF; -.
DR Proteomes; UP000002493; Chromosome 1.
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..443
FT /note="Probable D-serine dehydratase"
FT /id="PRO_0000185623"
FT MOD_RES 118
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 443 AA; 48297 MW; 35C182294A32BA6A CRC64;
MNKLNVEVLK KQFPLVEQLI NLDEVCWFNP NVTSLEEGLP HVGLNAEDIH VASARLKRFA
PYLMKAFPET KAASGLIESP VVDIPKMKAA LETQYNVPIF GRLMLKLDSH LPISGSIKAR
GGIYEVLVHA EKLAIATGLL SESDDYSKLL SGEFRQFFQQ YSIAVGSTGN LGMSIGMMSA
KLGFSVSVHM SADAREWKKN KLRSHGVNVV EYEQDYGVAV EQGRKQAESD PNCFFIDDEN
SQTLFLGYSV AGERLKQQFD DLGIVVDERH PLFVYLPCGV GGGPGGVAFG LKVAFGDHVH
CIFAEPTHSP CMLLGVHTGL HDEIAVQDIG IDNLTAADGL AVGRPSGFVG RAMERLIDGY
YTVTDERMYQ LLGELSEREG INLEPSALAG MMGAVHVSGS LHYQTRLQLT DERLKNATHL
VWATGGGMVP EAEMSADLAK SGR
