SDHD_BACCR
ID SDHD_BACCR Reviewed; 443 AA.
AC Q81F73;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=BC_1725;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(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 -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01030}.
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DR EMBL; AE016877; AAP08701.1; -; Genomic_DNA.
DR RefSeq; NP_831500.1; NC_004722.1.
DR RefSeq; WP_000658539.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81F73; -.
DR SMR; Q81F73; -.
DR STRING; 226900.BC_1725; -.
DR EnsemblBacteria; AAP08701; AAP08701; BC_1725.
DR KEGG; bce:BC1725; -.
DR PATRIC; fig|226900.8.peg.1713; -.
DR HOGENOM; CLU_035707_0_0_9; -.
DR OMA; ESDPNCF; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0036088; P:D-serine catabolic process; IBA:GO_Central.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
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..443
FT /note="Probable D-serine dehydratase"
FT /id="PRO_0000185602"
FT MOD_RES 116
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 443 AA; 49063 MW; E804AB78FC45C342 CRC64;
MKEIGALQAE YPLVNKLIAT EEVFWINPNI EKYETAIKDS PLNEENVKDA EERLKRFAPY
IAKVFPETKG ANGIIESPLV KIPSMKEALE RKYEQPILGE LLLKCDSHLP ISGSIKARGG
IYEVLKHAEQ LALQHGMVTE EDNYSVLDSD TCREFFSKYS IAVGSTGNLG LSIGIMSANL
GFNVTVHMSA DAKEWKKDLL RSKGVNVIEY EDDYSKAVEE GRRQADADPS CYFVDDENSH
DLFLGYAVAA SRLQKQLEEL EVVVDENHPL FVYLPCGVGG GPGGVAFGLK LLYKDNVHCY
FAEPTHSPCM LLGLMTGLHD KISVQDIGID NVTDADGLAV GRPSGFVGKT MEPFLSGNYT
VSDEELYRLL KELADTENIY LEPSALAGMI GPVKVCKEDE YLQKLQLTEK VKKGTHIVWG
TGGSMVPNDT MDEYYRKGLE LTI