SDHD_HISS2
ID SDHD_HISS2 Reviewed; 438 AA.
AC B0UWV3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=HSM_1892;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-2008) 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: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}.
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DR EMBL; CP000947; ACA31680.1; -; Genomic_DNA.
DR RefSeq; WP_012340977.1; NC_010519.1.
DR AlphaFoldDB; B0UWV3; -.
DR SMR; B0UWV3; -.
DR STRING; 228400.HSM_1892; -.
DR EnsemblBacteria; ACA31680; ACA31680; HSM_1892.
DR KEGG; hsm:HSM_1892; -.
DR HOGENOM; CLU_035707_0_0_6; -.
DR OMA; ESDPNCF; -.
DR OrthoDB; 912282at2; -.
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_1000084240"
FT MOD_RES 114
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 438 AA; 48531 MW; D5683D1CCABDCC6E CRC64;
MKIQHLMQDP FIQKLMRFEE VMWFNPKSAG VKTGLSYVGL DVSDTQQAAE RLQRFAPYFC
RAFPETQKTK GILESELVSI DKMKSALIDH YHMPIQGRLL LKKDSHLPIS GSIKARGGIY
EVLAYAEKLA LEHHLITESD 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