SDHD_HAES1
ID SDHD_HAES1 Reviewed; 438 AA.
AC Q0I5V1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Probable D-serine dehydratase {ECO:0000255|HAMAP-Rule:MF_01030};
DE EC=4.3.1.18 {ECO:0000255|HAMAP-Rule:MF_01030};
DE AltName: Full=D-serine deaminase {ECO:0000255|HAMAP-Rule:MF_01030};
DE Short=DSD {ECO:0000255|HAMAP-Rule:MF_01030};
GN Name=dsdA {ECO:0000255|HAMAP-Rule:MF_01030}; OrderedLocusNames=HS_1718;
OS Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=205914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129Pt;
RX PubMed=17172329; DOI=10.1128/jb.01422-06;
RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA Xie G., Inzana T.J.;
RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT influenzae Rd.";
RL J. Bacteriol. 189:1890-1898(2007).
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:0000255|HAMAP-Rule:MF_01030};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01030};
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01030}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI25986.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000436; ABI25986.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041604425.1; NC_008309.1.
DR AlphaFoldDB; Q0I5V1; -.
DR SMR; Q0I5V1; -.
DR STRING; 205914.HS_1718; -.
DR EnsemblBacteria; ABI25986; ABI25986; HS_1718.
DR KEGG; hso:HS_1718; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_6; -.
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; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR48078:SF9; PTHR48078:SF9; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR02035; D_Ser_am_lyase; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate.
FT CHAIN 1..438
FT /note="Probable D-serine dehydratase"
FT /id="PRO_0000291732"
FT MOD_RES 114
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 438 AA; 48558 MW; DEB359375D95687C CRC64;
MKIQHLMQDP FIQKLMRFEE VMWFNPKSAG VKTGLSYVGL DVSDTQQAAE RLQRFAPYFC
RAFPETQKTK GILESELVSI DKMKSALIDH YHMPIQGRLL LKKDSHLPIS GSIKARGGIY
EVLAYAEKLA LEHHLITEND DYSQLCDEKI KDFFSRYSIA VGSTGNLGLS IGIMGAVLGF
KVSVHMSADA REWKKQKLRS YGVNVVEYTQ DYGVAVAQGR KAALSDPNCF FIDDENSTTL
FLGYSVAGQR LKQQFLEQGI KVDENHPLFV YLPCGVGGGP GGVAFGLKLA FGDYVHCIFA
EPTHSPCMLL GVYTGLHDKI AVQDLGIDNI TAADGLAVGR ASGFVGRAME HLLDGFYTIE
DQKLYDLLGL LHKTENIQLE PSALAGMIGP LHINHSDYLR RYHITQEQLA NATHIVWATG
GGMVPDVEMQ KYLSLGRF
