ID SDHD_PHOLL Reviewed; 443 AA.
AC Q7N5H9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 105.
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=plu1970;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01) (Photorhabdus luminescens subsp. laumondii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(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 -!- 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; BX571865; CAE14263.1; -; Genomic_DNA.
DR RefSeq; WP_011146231.1; NC_005126.1.
DR AlphaFoldDB; Q7N5H9; -.
DR SMR; Q7N5H9; -.
DR STRING; 243265.plu1970; -.
DR GeneID; 24166670; -.
DR KEGG; plu:plu1970; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_6; -.
DR OrthoDB; 9780546at2; -.
DR Proteomes; UP000002514; 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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR02035; D_Ser_am_lyase; 1.
DR PANTHER; PTHR48078:SF9; D-SERINE DEHYDRATASE; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 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="D-serine dehydratase"
FT /id="PRO_0000185616"
FT MOD_RES 118
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 443 AA; 48332 MW; 87F2AB6BF74316F2 CRC64;
MKRTEIQQLL NEYPLVKNLM ELEEIFWFNP CNTTLKEGLP FVGLGADDVE DAEARLDRFA
SYLCKAFPET AVTHGIIESE IVAIPTMQKT LEQHYGVGIT GRILLKKDSH LPISGSIKAR
GGIYEVLTHA EKLALQAGLL AENDDYSKLF SEELRRFFNQ YSIAVGSTGN LGLSIGIASA
KLGFNVSVHM SADAREWKKQ KLRSHGVNVV EHELDYGVAV ARGRKEAESA PNCFFIDDEN
SQTLFLGYSV AGGRVKAQFE QMNIVVDEDH PLFVYLPCGV GGGPGGVAFG LKLAFGDHVH
CIFAEPTHSP SMLLGVYTGL HDNICVQDIG IDNITAADGL AVGRASGFVG RAMERLLDGF
YTVQDQEMYN LLGLLDRDEG IRLEPSALVG MAGPARVSGN LDYLNNKNLS AEKMKQATHL
VWATGGGMVP DDEMTKYLAT AKI
//
