SDHD_PSEMY
ID SDHD_PSEMY Reviewed; 446 AA.
AC A4XXF3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Pmen_3266;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000680; ABP86019.1; -; Genomic_DNA.
DR RefSeq; WP_012019367.1; NC_009439.1.
DR AlphaFoldDB; A4XXF3; -.
DR SMR; A4XXF3; -.
DR STRING; 399739.Pmen_3266; -.
DR PRIDE; A4XXF3; -.
DR EnsemblBacteria; ABP86019; ABP86019; Pmen_3266.
DR KEGG; pmy:Pmen_3266; -.
DR PATRIC; fig|399739.8.peg.3313; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_6; -.
DR OMA; ESDPNCF; -.
DR OrthoDB; 912282at2; -.
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_1000063714"
FT MOD_RES 118
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 446 AA; 48120 MW; 78ABFB717C300E30 CRC64;
MILGQPLAQW RAQYPLLDEL IALRETSWFN PAVAPAAEAL GDVGLSAADV ADARARLERF
APYLARAFPQ TAASGGIIES DILPLPQMQA LLREEAEGEI GALWLKRDSH LPISGSIKAR
GGIYEVLKHA EDLALAAGLL GLDDDYACLD SDAMRAFFGG YQVAVGSTGN LGLSIGIISA
RLGFQATVHM SADARQWKKD KLRAHGVTVV EYASDYSVAV EQGRRQAEAD PRCHFVDDEN
SRHLFLGYAV AGERLRQQLA AANVVVDAEH PLFVYLPCGV GGGPGGVAFG LKLAFGDAVH
CLFAEPTHSP CMLLGVHTGR HEELAVQDFG IDNRTAADGL AVGRPSGFVG RAMQRLIDGY
YTVSDEQLFR YLALVEQTEG QRLEPSALAG MPGVLRVLGE RQGYRQRMGL TPQRMARATH
LVWATGGSMV PEAEMDSYLA RGRQLL
