SDHD_OENOB
ID SDHD_OENOB Reviewed; 433 AA.
AC Q04G28;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 78.
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=OEOE_0657;
OS Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=203123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-331 / PSU-1;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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=ABJ56594.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000411; ABJ56594.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041346443.1; NC_008528.1.
DR AlphaFoldDB; Q04G28; -.
DR SMR; Q04G28; -.
DR STRING; 203123.OEOE_0657; -.
DR DNASU; 4416798; -.
DR EnsemblBacteria; ABJ56594; ABJ56594; OEOE_0657.
DR KEGG; ooe:OEOE_0657; -.
DR PATRIC; fig|203123.7.peg.665; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_9; -.
DR OrthoDB; 912282at2; -.
DR Proteomes; UP000000774; 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; 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; Reference proteome.
FT CHAIN 1..433
FT /note="Probable D-serine dehydratase"
FT /id="PRO_0000291734"
FT MOD_RES 110
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 433 AA; 48272 MW; C36355D401651420 CRC64;
MTETLLKKKL NLNDQFLLNL KNYQEIFWKN PNYGDELPDL DVNRETIFQA NRRLERFAPY
LESVFSDTKR SKGIIESPIQ RMDSIKDLLS VKGSLLIKRD DLMPVSGSIK SRGGIYEVLC
FAEKIAIENG FDLKKDNYQD LRKDKYRKLF NQWRIEVAST GNLGLSVGLM ASTLGFKARI
HMSHDATDWK INKLLQNGVE VKIYDDNFSN AVAAARVSSQ RDPYSYFIDD EGSKLLFAGY
ATAGERVKKQ LSKMQIEVSK EHPLVVYLPA GVGGSPSGVA FGLKLQFADA VIPIFVEPTH
MPSVLLGMAS GLNHDISVYD IGIDGKTAAD GLAVGRPSMI AGKYMKDKLF GIATVSDSDM
FAYQGMLKKL ENIEVEPSAA VGIRGLIQSK EISEIPDSAT HMVWATGGSM VPKNTMHKYE
DKAVRIFNTW KSE