SDHD_VIBC3
ID SDHD_VIBC3 Reviewed; 441 AA.
AC A5F0M6; C3M6G8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
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};
GN OrderedLocusNames=VC0395_0362, VC395_A0899;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000626; ABQ18955.1; -; Genomic_DNA.
DR EMBL; CP001236; ACP11731.1; -; Genomic_DNA.
DR RefSeq; WP_001885353.1; NZ_JAACZH010000012.1.
DR AlphaFoldDB; A5F0M6; -.
DR SMR; A5F0M6; -.
DR STRING; 345073.VC395_A0899; -.
DR EnsemblBacteria; ABQ18955; ABQ18955; VC0395_0362.
DR GeneID; 57742247; -.
DR KEGG; vco:VC0395_0362; -.
DR KEGG; vcr:VC395_A0899; -.
DR PATRIC; fig|345073.21.peg.3629; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_6; -.
DR OMA; ESDPNCF; -.
DR Proteomes; UP000000249; 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.
FT CHAIN 1..441
FT /note="Probable D-serine dehydratase"
FT /id="PRO_1000072954"
FT MOD_RES 118
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 441 AA; 48333 MW; 73AC3ED27F7348AB CRC64;
MMTINIEQLT EQYPLVKELI ELKEVSWFNP SITRLEEGLS YVGLGSEDIQ DASQRLKRFA
PYLAKAFPET AKTNGIIESE VVPISEMQSV LEREYDTPIQ GRLLLKKDSH LPISGSIKAR
GGIYEVLTHA EKLAIEAGLL TESDDYSKLL NEEFRDFFKR FSIAVGSTGN LGMSIGIMSA
KLGFSVSVHM SADARAWKKN RLRALGVNVI EYAQDYGVAV AQGRKEAEND PTCFFIDDEN
SQTLFLGYSV AGERLKKQFD EKGIVVDAQH PLFVYLPCGV GGGPGGVAFG LKMAFGDNVH
CIFAEPTHSP CMMLGVHTGL HDAISVQDIG IDNITAADGL AVGRASGFVG RAMERLLDGY
LTISDERMYR LLGQLNEAEN IQLEPSALAG MIGPIVVTKS VEYRARMQFD DTVMGNATHL
VWATGGGMVP AEEMDSYLKN R