SDHD_PHOPR
ID SDHD_PHOPR Reviewed; 443 AA.
AC Q6LHF5;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=PBPRB1408;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(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; CR378679; CAG23275.1; -; Genomic_DNA.
DR RefSeq; WP_011221451.1; NC_006371.1.
DR AlphaFoldDB; Q6LHF5; -.
DR SMR; Q6LHF5; -.
DR STRING; 298386.PBPRB1408; -.
DR EnsemblBacteria; CAG23275; CAG23275; PBPRB1408.
DR KEGG; ppr:PBPRB1408; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_6; -.
DR OMA; ESDPNCF; -.
DR OrthoDB; 912282at2; -.
DR Proteomes; UP000000593; Chromosome 2.
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_0000185617"
FT MOD_RES 118
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 443 AA; 48350 MW; E9CFB74F6E63FBE5 CRC64;
MSTLNIQQLV TEFPLVEKLI ALDDVSWFNP NITTLAEGLP YVGLDKTDIK DASDRLKRFA
PYLAKAFPET AKTNGIIESD VVAIPAMKTV LEQQYHIAIQ GTLLLKKDSH LPISGSIKAR
GGIYEVLTHA EKLAIQAGLL SESDDYSKLF TDEFRAFFKQ FSIAVGSTGN LGMSIGIMSA
KIGFSVSVHM SADARQWKKD KLRSHGVIVV EYKEDYGVAV AQGRKEAEKD PTCFFIDDEN
SPTLFLGYSV AGERLKSQFE AMNILVDELH PLFVYLPCGV GGGPGGVAFG LKMAFGDNVH
CIFAEPTHSP CMLLGIHTGL HDEISVQDIG IDNITAADGL AVGRGSGFVG RAMERLLDGF
YTISDERMYH HLGEMSKYED IQLEPSALAG MLGPVVVSDN EEYLQRIQMD EQKLKNATHL
VWATGGGMVP SEEMASYLAK SGI
