SDHD_VIBCH
ID SDHD_VIBCH Reviewed; 441 AA.
AC Q9KL72;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=VC_A0875;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003853; AAF96773.1; -; Genomic_DNA.
DR PIR; C82406; C82406.
DR RefSeq; NP_233261.1; NC_002506.1.
DR RefSeq; WP_001885353.1; NZ_LT906615.1.
DR AlphaFoldDB; Q9KL72; -.
DR SMR; Q9KL72; -.
DR STRING; 243277.VC_A0875; -.
DR DNASU; 2612586; -.
DR EnsemblBacteria; AAF96773; AAF96773; VC_A0875.
DR GeneID; 57742247; -.
DR KEGG; vch:VC_A0875; -.
DR PATRIC; fig|243277.26.peg.3491; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_6; -.
DR OMA; ESDPNCF; -.
DR BioCyc; VCHO:VCA0875-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0036088; P:D-serine catabolic process; IBA:GO_Central.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
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..441
FT /note="Probable D-serine dehydratase"
FT /id="PRO_0000185622"
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