SDHD_GEOKA
ID SDHD_GEOKA Reviewed; 441 AA.
AC Q75TC9; Q5KYM9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=GK1922;
GN ORFNames=GKB09;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15168170; DOI=10.1007/s00792-004-0394-3;
RA Takami H., Nishi S., Lu J., Shimamura S., Takaki Y.;
RT "Genomic characterization of thermophilic Geobacillus species isolated from
RT the deepest sea mud of the Mariana Trench.";
RL Extremophiles 8:351-356(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; AB126619; BAD18349.1; -; Genomic_DNA.
DR EMBL; BA000043; BAD76207.1; -; Genomic_DNA.
DR RefSeq; WP_011231408.1; NC_006510.1.
DR AlphaFoldDB; Q75TC9; -.
DR SMR; Q75TC9; -.
DR STRING; 235909.GK1922; -.
DR EnsemblBacteria; BAD76207; BAD76207; GK1922.
DR KEGG; gka:GK1922; -.
DR PATRIC; fig|235909.7.peg.2061; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_9; -.
DR OMA; ESDPNCF; -.
DR Proteomes; UP000001172; 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; 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_0000291731"
FT MOD_RES 101
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 441 AA; 49082 MW; 540C62A7F01ACEB9 CRC64;
MIMAAEEVFW RNPKYHAFAQ AIRTIPLRER DVKEAEERLR RFAPYIAKVF PETQPAHGII
ESPLVRIPNM QRRLEKMFQT NIEGDLLLKC DSHLPISGSI KARGGIYEVL KHAEDLALAN
GMIAIGEDYA VMASEEFRQF FSRYSLVVGS TGNLGLSIGI IGAQLGFRVT VHMSADAKQW
KKDLLRSKGV TVIEHLTDYN KVVEEARRQS AEDPTSYFID DENSIHLFLG YAVAAFRLKK
QLEDMNITVD ETHPLFVYLP CGVGGGPGGV TFGLKLVYGD HVHCFFAEPT HSPCMLLGLM
TGEHDRVSVQ DFGLDNKTEA DGLAVGRPSR LVGNMLENVI SGVYTVDDST LYRLLAAMVE
TEEIYLEPSA LAGVAGPVRL FRDSAGQTYV EENDLKEKMK NAVHICWATG GSMVPKGVME
AYYREGMRIE TMTGNCFSEG R