ID A0A2A9FZ82_9VIBR Unreviewed; 443 AA.
AC A0A2A9FZ82;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=ATG66_2314 {ECO:0000313|EMBL:PFG55991.1};
OS Vibrio sp. ES.051.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1761909 {ECO:0000313|EMBL:PFG55991.1, ECO:0000313|Proteomes:UP000223114};
RN [1] {ECO:0000313|EMBL:PFG55991.1, ECO:0000313|Proteomes:UP000223114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES.051 {ECO:0000313|EMBL:PFG55991.1,
RC ECO:0000313|Proteomes:UP000223114};
RA Fredrickson J.;
RT "Microbial Interactions in Extremophilic Mat Communities.";
RL Submitted (OCT-2017) 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:PFG55991.1}.
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DR EMBL; PDJL01000004; PFG55991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9FZ82; -.
DR OrthoDB; 9780546at2; -.
DR Proteomes; UP000223114; 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:PFG55991.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01030}.
FT DOMAIN 75..396
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 118
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01030"
SQ SEQUENCE 443 AA; 48615 MW; 790E9CF6AB9AE192 CRC64;
MIKQNMETLT KQFPLLEQLI ELKEVCWFNP NITSLVEALP YVGLGEKDIQ AASERLTRFA
PYLEKAFPET ARSNGIIESP MVDIEAMKAH LEKQYGTRIL GRLMLKKDSH LPISGSIKAR
GGIYEVLAHA EKLAFDAGLL CESDDYSKLL GEEFRQFFRQ YNIAVGSTGN LGMSIGIMSA
TLGFSVSVHM SADAREWKKN KLRSHGVNVV EYQQDYGVAV DQGRKEAEQD PNCFFIDDEN
SQTLFLGYSV AGERLKQQFD ALGVVIDENH PLFVYLPCGV GGGPGGVAFG LKMAFGDHVH
CIFAEPTHSP CMLLGVHTGL HDEIAVQDLG IDNMTAADGL AVGRASGFVG RAMERLIDGY
YTITDERMYR HLGELSELEE IRLEPSALAG MIGAVHVSNG REYQARMAIT EGTLKNAIHL
VWATGGGMVP DAEMAAYLAK SGR
//
