ID A0A396S974_9BACI Unreviewed; 439 AA.
AC A0A396S974;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=D1B33_09015 {ECO:0000313|EMBL:RHW37655.1};
OS Lysinibacillus yapensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=2304605 {ECO:0000313|EMBL:RHW37655.1, ECO:0000313|Proteomes:UP000265692};
RN [1] {ECO:0000313|EMBL:RHW37655.1, ECO:0000313|Proteomes:UP000265692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-03 {ECO:0000313|EMBL:RHW37655.1,
RC ECO:0000313|Proteomes:UP000265692};
RA Yu L.;
RT "Lysinibacillus sp. YLB-03 draft genome sequence.";
RL Submitted (AUG-2018) 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:RHW37655.1}.
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DR EMBL; QWEI01000003; RHW37655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A396S974; -.
DR OrthoDB; 9780546at2; -.
DR Proteomes; UP000265692; 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:RHW37655.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01030}; Reference proteome {ECO:0000313|Proteomes:UP000265692}.
FT DOMAIN 95..397
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 439 AA; 49756 MW; 8E1E6DAEBB8DA273 CRC64;
MIEKQKLDDL IKKNEKLNDI ISSKPVLWFN PQKQKQQKSQ SQFSFEDVLE AEQRLQRFSS
YIRVAFPETE SLQGIIESEI KEIPSMKKAI ENEYTSELPG RIFLKCDFAL PISGSIKARG
GIYEVLKYAE QLAIEHRLIQ YNDDYAKFNE EEFYEFFRQY KIAVGSTGNL GLSIGIMGAK
LGFQVTVHMS SDAKEWKKQL LREKGVEVIE YSSDYSKAVE EGRKQAELDP MCHFIDDENS
RDLFAGYAVA ATRLKKQLKE ENIRVDEEHP LFVYLPCGVG GGPGGVAFGL KQIYGDHVHL
FFGEPTQSPC MLVGMMTGLH DEISVGDLGL SNRTEADGLA VGRASKFVGK MMEPVLSGCY
TVDDEFLFKS LKLMMEREEI FMEPSAHAGV YGVISLMKEG EEYIRQNHLN MDKATHLVWS
TGGNMVPLTE RELMLNKKI
//
