ID   SDHD_ACIBC              Reviewed;         444 AA.
AC   B2HVC6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=ACICU_00935;
OS   Acinetobacter baumannii (strain ACICU).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=405416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACICU;
RX   PubMed=18411315; DOI=10.1128/aac.01643-07;
RA   Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA   Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT   "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT   Acinetobacter baumannii strain belonging to the European clone II group.";
RL   Antimicrob. Agents Chemother. 52:2616-2625(2008).
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; CP000863; ACC56247.1; -; Genomic_DNA.
DR   RefSeq; WP_000994873.1; NZ_CP031380.1.
DR   AlphaFoldDB; B2HVC6; -.
DR   SMR; B2HVC6; -.
DR   KEGG; abc:ACICU_00935; -.
DR   HOGENOM; CLU_035707_0_0_6; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000008839; 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..444
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_1000213343"
FT   MOD_RES         118
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   444 AA;  49082 MW;  9F52515D5D44CDD8 CRC64;
     MNAVQIDQLK QQFPLIETLQ AYQETFWFNP HRYPLNEALA KVCLTEQDVK EAEARLARFA
     PYLAKVFPET QAQHGKIESA LVEIAEMQQA LSLQKHKTLT GKLWLKKDSH LPISGSIKAR
     GGIYEVLAHA EKLAIEAGLL KLEDDYSKLD QDSFRTFFSK YQIAVGSTGN LGLSIGIMSA
     KLGFRVSVHM SADARQWKKD KLRSLGVNVV EYASDYGVAV EEGRKAAEQD PFCFFIDDEN
     STTLFLGYAV AGLRLKQQFE QKQIKVDADH PLFVYLPCGV GGGPGGVSFG LKLAFGEHVH
     CIFAEPTHSP CMLLGVYTGL HDQISVNDIG LDNITAADGL AVGRASGFVG RAMQQLIDGY
     YTIHDECLYE LIALLNQTEN IQVEPSAAAG MMGPYYVQTT PDYLALHQLS AEKLQHATHV
     VWATGGGMVP PDEMQKYLTY SQRN