SDHD_BURL3
ID SDHD_BURL3 Reviewed; 446 AA.
AC Q396Y3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=Bcep18194_B1364;
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000152; ABB11478.1; -; Genomic_DNA.
DR AlphaFoldDB; Q396Y3; -.
DR SMR; Q396Y3; -.
DR EnsemblBacteria; ABB11478; ABB11478; Bcep18194_B1364.
DR KEGG; bur:Bcep18194_B1364; -.
DR PATRIC; fig|482957.22.peg.5050; -.
DR HOGENOM; CLU_035707_0_0_4; -.
DR OMA; ESDPNCF; -.
DR Proteomes; UP000002705; 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; 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.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate.
FT CHAIN 1..446
FT /note="Probable D-serine dehydratase"
FT /id="PRO_0000291721"
FT MOD_RES 113
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 446 AA; 46952 MW; F3899D1468B15907 CRC64;
MRYRSMTVTL QPADLLARLQ SRHPLLWLNP HAGSPLPHDA PGPGAIATAE ARLARCEPLM
AELFPELATS AGKIESPLMP ADNLQRTLSL PADTHGAWFI KRDDALPIAG SIKARGGFHE
VLALAESIAI EHGLLEPAGD RRILASAAAR ERFAAHTVIV GSTGNLGLSI GVMASALGFE
SVVHMSTDAK PWKKARLRQR GVRVIEHDGD YAQAVAAGRA QARNQPRSHF VDDEGSLMLF
LGYAASARHL AAQLAEAGRR VDATHPLFVH IPCGVGGAPG GIAHGLKALF GEHVHCFFAE
PVASPCMLVQ LAAGLGKPVS VYDVGLDNRT EADGLAVAQA SHLVSPLMAS LLSGVFTVSD
AQLYAQLLAV QHATGVELEP SAAAAVGGPG WLTRSPAGRD YVHRHAIDLR QSTHVIWATG
GSLVPPEEHR RFQSHAKALA GAAAGT
