SDHD_BURP1
ID SDHD_BURP1 Reviewed; 445 AA.
AC Q3JJ76;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=BURPS1710b_A1220;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000125; ABA52188.1; -; Genomic_DNA.
DR RefSeq; WP_004529338.1; NC_007435.1.
DR AlphaFoldDB; Q3JJ76; -.
DR SMR; Q3JJ76; -.
DR EnsemblBacteria; ABA52188; ABA52188; BURPS1710b_A1220.
DR KEGG; bpm:BURPS1710b_A1220; -.
DR HOGENOM; CLU_035707_0_0_4; -.
DR OMA; ESDPNCF; -.
DR OrthoDB; 912282at2; -.
DR Proteomes; UP000002700; Chromosome II.
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..445
FT /note="Probable D-serine dehydratase"
FT /id="PRO_0000291720"
FT MOD_RES 111
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 445 AA; 46292 MW; F4E22B08A8B6EAD6 CRC64;
MPVGRSLSLD PNLLAQLQSH SPTLWLNPHQ GMPLPDFAPT AADLADADAR LRRCAGLLAE
LFAELRPSGG LIASPLQPAE PLKRAARAGH AQAGAWYVKR DDALPVAGSI KARGGFHEVL
ALAESIAERH GLAGADTDRR ALASGAARAR FARHTVMVGS TGNLGLSIGM LASALGFRTV
AHMSADAKAW KKARLRTRGV EVVEHAGDYA KAVDAGRRQA AGMPCCHFVD DEGSRMLFLG
YATAAAELAA QLAQAGRPVD ARHPLFVHLP CGVGGAPGGI VYGLKALYGE HVHAFVAEPT
ASPCVLVQLA GDAAHPRSVY DIGLDNRTEA DGLAVAQASP LAAALLRAQA AGAFTVDDRQ
LFAHLLDARE RLGIDLEPSA AAAFGGPAWI AGSDAGRAYL RGRGIDPDAA THVIWATGGS
LVPAQEHRRF QAHARAQRQV GGAGA