ID   SDHD_ACIB5              Reviewed;         444 AA.
AC   B7I8P7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=AB57_1052;
OS   Acinetobacter baumannii (strain AB0057).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=480119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB0057;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(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; CP001182; ACJ40841.1; -; Genomic_DNA.
DR   RefSeq; WP_000859908.1; NC_011586.2.
DR   AlphaFoldDB; B7I8P7; -.
DR   SMR; B7I8P7; -.
DR   KEGG; abn:AB57_1052; -.
DR   HOGENOM; CLU_035707_0_0_6; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000007094; 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_1000213342"
FT   MOD_RES         118
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   444 AA;  49053 MW;  2FD18D4AF74802E8 CRC64;
     MKTVQLDQLK QQFPLIQTLQ DYQETFWFNP HRYPLNEALA KVGLTEQDVK EAEARLARFA
     PYLAKVFPET QAQYGKIESA LVKIADMQQA 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
     LWATGGGMVP PDEMQKYLTH SQSN