SDHD_FUSNN
ID SDHD_FUSNN Reviewed; 441 AA.
AC Q8RFX6;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=FN0553;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL94749.1; -; Genomic_DNA.
DR RefSeq; NP_603450.1; NC_003454.1.
DR AlphaFoldDB; Q8RFX6; -.
DR SMR; Q8RFX6; -.
DR STRING; 190304.FN0553; -.
DR PRIDE; Q8RFX6; -.
DR EnsemblBacteria; AAL94749; AAL94749; FN0553.
DR KEGG; fnu:FN0553; -.
DR PATRIC; fig|190304.8.peg.1120; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_0; -.
DR InParanoid; Q8RFX6; -.
DR OMA; ESDPNCF; -.
DR BioCyc; FNUC190304:G1FZS-1142-MON; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0036088; P:D-serine catabolic process; IBA:GO_Central.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
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; 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.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..441
FT /note="Probable D-serine dehydratase"
FT /id="PRO_0000185614"
FT MOD_RES 115
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 441 AA; 49954 MW; E2058AF21B4851E2 CRC64;
MDIKNMIINN PLIKNMIDKK EVGWTNPKEM NYTEYEKKLP LKDQELKEAE ERLKRFAPFI
KKVFPETEET YGIIESPLEE IFNMQKELEK KYHTEILGKL YLKMDSHLPV AGSIKARGGV
YEVLKHAEEL AMEAGLLKLE DDYSILADKK FKDFFSKYKI QVGSTGNLGL SIGITSAALG
FQVIVHMSAD AKKWKKDMLR SKGVQVIEYE SDYGKAVEEG RKNSDADPMS YFVDDEKSMN
LFLGYTVAAS RIKKQFDKKG IVINKEHPLI VYIPCGVGGA PGGVAYGLKR IFKENVYIFF
VEPVLAPCML LGMQTGLHEK ISVYDVGIHG ITHADGLAVA RPSGLVGRLM EPILSGIFTV
DDYKLYDYLR ILNETENKRI EPSSCAAFEG VVSLLKYEDS KKYIENRIGK NINNVYHVCW
ATGGKMVPQE DMEIFLNTYL K