ID A0A136WD75_9FIRM Unreviewed; 444 AA.
AC A0A136WD75;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Probable D-serine dehydratase {ECO:0000256|HAMAP-Rule:MF_01030};
DE EC=4.3.1.18 {ECO:0000256|HAMAP-Rule:MF_01030};
DE AltName: Full=D-serine deaminase {ECO:0000256|HAMAP-Rule:MF_01030};
DE Short=DSD {ECO:0000256|HAMAP-Rule:MF_01030};
GN Name=dsdA {ECO:0000256|HAMAP-Rule:MF_01030,
GN ECO:0000313|EMBL:KXL52465.1};
GN ORFNames=CLNEO_21610 {ECO:0000313|EMBL:KXL52465.1};
OS Anaerotignum neopropionicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerotignum.
OX NCBI_TaxID=36847 {ECO:0000313|EMBL:KXL52465.1, ECO:0000313|Proteomes:UP000070539};
RN [1] {ECO:0000313|EMBL:KXL52465.1, ECO:0000313|Proteomes:UP000070539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM-3847 {ECO:0000313|EMBL:KXL52465.1,
RC ECO:0000313|Proteomes:UP000070539};
RA Poehlein A., Beck M.H., Bengelsdorf F.R., Daniel R., Duerre P.;
RT "Genome sequence of Clostridium neopropionicum X4, DSM-3847.";
RL Submitted (JAN-2016) 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:0000256|HAMAP-Rule:MF_01030};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01030};
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01030}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXL52465.1}.
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DR EMBL; LRVM01000007; KXL52465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136WD75; -.
DR STRING; 36847.CLNEO_21610; -.
DR PATRIC; fig|36847.3.peg.2531; -.
DR Proteomes; UP000070539; Unassembled WGS sequence.
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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR02035; D_Ser_am_lyase; 1.
DR PANTHER; PTHR48078:SF9; D-SERINE DEHYDRATASE; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01030, ECO:0000313|EMBL:KXL52465.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01030}; Reference proteome {ECO:0000313|Proteomes:UP000070539}.
FT DOMAIN 99..393
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 117
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01030"
SQ SEQUENCE 444 AA; 49413 MW; 6DA8B7C08D3C3D00 CRC64;
MDQELWNQMN NKELLKDVSN GKEVVWVNEN LKTAEMALPE IEVTMKDIDD AEARLARFAP
FILKVFPETA PENGLIESPF TEIKKMKHQL EKEYNTTIPG RLFLKQDSHL AISGSIKARG
GIYEVLKHAE DLAISHNMLK ESDDYSIFAS KEFKEFFSKF KIQVGSTGNL GMSIGIMSAV
LGFHVIVHMS ADAKQWKKDL LRKRGAEVIE YNDDYSKAVE VGRKNSDADP TSYFVDDENS
VTLFLGYAVA AKRIKKQFEE QGIVIDEEHP LFVYIPCGVG GAPGGVAFGL KQFFGDNVHI
FFVEPTQAPC MLVGMASGLQ NKVCVQDFGL TGQTHADGLA VGRASGFVGG VMKHMLSGIF
SLEDYHIYDL MRDIVNSQTI FLEPSACAAF WGPIQLMKEP ATKAYIEKMG LSQKMPNAIH
VPWATGGSLV PAEIREEYMH THLK
//
