SDHD_BACAH
ID SDHD_BACAH Reviewed; 446 AA.
AC A0RCF8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 71.
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=BALH_1568;
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam;
RX PubMed=17337577; DOI=10.1128/jb.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABK84901.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000485; ABK84901.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000658358.1; NC_008600.1.
DR AlphaFoldDB; A0RCF8; -.
DR SMR; A0RCF8; -.
DR EnsemblBacteria; ABK84901; ABK84901; BALH_1568.
DR KEGG; btl:BALH_1568; -.
DR HOGENOM; CLU_035707_0_0_9; -.
DR Proteomes; UP000000761; 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.
FT CHAIN 1..446
FT /note="Probable D-serine dehydratase"
FT /id="PRO_0000291719"
FT MOD_RES 116
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 446 AA; 49564 MW; 9B37C3929E481921 CRC64;
MKEIEKLKEE YPLLNKLIET EEVLWVNPNM EKYETAIKDS PLSEENVKDA KERLKRFASY
IAKVFPETKE TKGIIESPLL KIPSMKQALE KNYEQPILGE LLLKCDSHLP ISGSIKARGG
IYEVLKHAEQ LALQHGMLTE EDDYSILDSD TCREFFAKYS IAVGSTGNLG LSIGIMSAKL
GFNVTVHMSA DAKQWKKDLL RSKGVNVIEY EADYSKAVEE GRRQADADPS CYFVDDENSH
DLFLGYAVAA SRLQKQLEEL EIIVDEEHPL FVYLPCGVGG GPGGVAFGLK LLYKDNVHCF
FAEPTHSPCM LIGLMTGLHD KIAVQDIGID NVTDADGLAV GRPSGFVGKT MEPFLSGDYT
VSDEELYRLL KELADTENIY LEPSALAGMI GPVRVCKEDA YLQKQQLMEK VQKGTHIVWG
TGGSMVPEDV MNGYYKTGEA LTILEK