ID F6B5B2_DESCC Unreviewed; 431 AA.
AC F6B5B2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 OrderedLocusNames=Desca_1375 {ECO:0000313|EMBL:AEF94233.1};
OS Desulfotomaculum nigrificans (strain DSM 14880 / VKM B-2319 / CO-1-SRB)
OS (Desulfotomaculum carboxydivorans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=868595 {ECO:0000313|EMBL:AEF94233.1, ECO:0000313|Proteomes:UP000009226};
RN [1] {ECO:0000313|Proteomes:UP000009226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC {ECO:0000313|Proteomes:UP000009226};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL Submitted (MAY-2011) 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}.
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DR EMBL; CP002736; AEF94233.1; -; Genomic_DNA.
DR RefSeq; WP_013810148.1; NC_015565.1.
DR AlphaFoldDB; F6B5B2; -.
DR STRING; 868595.Desca_1375; -.
DR KEGG; dca:Desca_1375; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_9; -.
DR Proteomes; UP000009226; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01030, ECO:0000313|EMBL:AEF94233.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01030}; Reference proteome {ECO:0000313|Proteomes:UP000009226}.
FT DOMAIN 71..384
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 109
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01030"
SQ SEQUENCE 431 AA; 47336 MW; 8C2E0765322895FE CRC64;
MNEFNEKLLN QITKLNPVVW QNKKKETSDQ ALSKLDITYT DIIDAAERLN RFRPLISNLF
PETVNGIIES PLLAIPAMKK AMENLYQKDI GGRLYLKCDS HLKIAGSIKA RGGIYEVLKH
AETLAMAAGI LSPEDNYAKL AQPQFKDFFS RYKIAVGSTG NLGLSIGIIS SALGFQVTVH
MSADAKEWKK KLLRSKGVTV IEYSEDYSKA VAEGRKQCAA DPDCYFIDDE NSKDLFLGYS
VAALRLLDQL NKASITVDDR HPLYVYLPCG VGGAPGGITF GLKHIFKDNV NCYFVEPTHS
PCMILGLLTG KYDQLHVREY GIDNITEADG LAVGSPSKLV SHIAEKLIDG IYTISDDELF
KLLALLNDTE GIKIEPSAAA GLLGPTLLDT SQNATHICWA TGGLLLPDEI YSDMYHKGKG
LLNSIKTGIN R
//
