ID A0A2C6BWI2_9GAMM Unreviewed; 443 AA.
AC A0A2C6BWI2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=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:VFS46431.1};
GN ORFNames=CRN84_03675 {ECO:0000313|EMBL:PHI28490.1}, NCTC12282_01340
GN {ECO:0000313|EMBL:VFS46431.1};
OS Budvicia aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Budvicia.
OX NCBI_TaxID=82979 {ECO:0000313|EMBL:PHI28490.1, ECO:0000313|Proteomes:UP000224974};
RN [1] {ECO:0000313|Proteomes:UP000224974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_387 {ECO:0000313|Proteomes:UP000224974};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHI28490.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_387 {ECO:0000313|EMBL:PHI28490.1};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:VFS46431.1, ECO:0000313|Proteomes:UP000373449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12282 {ECO:0000313|EMBL:VFS46431.1,
RC ECO:0000313|Proteomes:UP000373449};
RG Pathogen Informatics;
RL Submitted (MAR-2019) 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 -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01030}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01030}.
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DR EMBL; PDDX01000001; PHI28490.1; -; Genomic_DNA.
DR EMBL; CAADJA010000002; VFS46431.1; -; Genomic_DNA.
DR RefSeq; WP_029093805.1; NZ_PDDX01000001.1.
DR AlphaFoldDB; A0A2C6BWI2; -.
DR STRING; 1111728.GCA_000427805_04516; -.
DR OrthoDB; 9780546at2; -.
DR Proteomes; UP000224974; Unassembled WGS sequence.
DR Proteomes; UP000373449; 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 CDD; cd06447; D-Ser-dehyd; 1.
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:PHI28490.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01030}; Reference proteome {ECO:0000313|Proteomes:UP000224974}.
FT DOMAIN 93..394
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; 48394 MW; 42A17B2274BA7E83 CRC64;
MKNTDIQTLI AEYPLVKQLI DLEEVSWFNP SVTTLEAGLP YVGLNASDVK QAEQRLNRFA
PYLCKAFPET QVTNGIIESQ VVAIPAMQKT LEQRYGIDIT GKILLKKDSH LPISGSIKAR
GGIYEVLTHA EKLAIQAGLL TESDDYSKLF SEEFKAFFGQ YSIAVGSTGN LGMSIGIMSA
KLGFSVSVHM SADAREWKKQ KLRSHGVKVV EYEQDYGVAV EQGRKEAESD PNCFFIDDEN
SQTLFLGYAV AGQRLKAQFS EMKVVVDENH PLFVYLPCGV GGGPGGVAFG LKLAFGDHVH
CIFAEPTHSP CMLLGVHTSL HDHISVQDIG IDNVTAADGL AVGRASGFVG RAMERLLDGY
YTISDREMYD LLGLLNREEG IQLEPSALAG MPGPSRVMAD AEYLKRMDLT PEKMSNSTHL
VWATGGGMVP QAEMEKYLAT AKI
//
