ID   FUCDH_XANCP             Reviewed;         300 AA.
AC   Q8P3K4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=2-keto-3-deoxy-L-fuconate dehydrogenase {ECO:0000303|PubMed:17144652};
DE            EC=1.1.1.- {ECO:0000269|PubMed:17144652};
GN   OrderedLocusNames=XCC4067;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC   {ECO:0000269|PubMed:17144652};
RX   PubMed=17144652; DOI=10.1021/bi061687o;
RA   Yew W.S., Fedorov A.A., Fedorov E.V., Rakus J.F., Pierce R.W., Almo S.C.,
RA   Gerlt J.A.;
RT   "Evolution of enzymatic activities in the enolase superfamily: L-fuconate
RT   dehydratase from Xanthomonas campestris.";
RL   Biochemistry 45:14582-14597(2006).
CC   -!- FUNCTION: Plays a role in the catabolism of L-fucose. Catalyzes the
CC       NAD(+)-dependent oxidation of 2-keo-3-deoxy-L-fuconate to 2,4-diketo-3-
CC       deoxy-L-fuconate. {ECO:0000269|PubMed:17144652}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.39 M for 2-keto-3-deoxy-L-fuconate
CC         {ECO:0000269|PubMed:17144652};
CC         KM=6.2 M for 2-keto-3-deoxy-L-galactonate
CC         {ECO:0000269|PubMed:17144652};
CC         KM=2.1 M for 2-keto-3-deoxy-D-arabinonate
CC         {ECO:0000269|PubMed:17144652};
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000255}.
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DR   EMBL; AE008922; AAM43288.1; -; Genomic_DNA.
DR   RefSeq; NP_639406.1; NC_003902.1.
DR   AlphaFoldDB; Q8P3K4; -.
DR   SMR; Q8P3K4; -.
DR   STRING; 340.xcc-b100_4269; -.
DR   EnsemblBacteria; AAM43288; AAM43288; XCC4067.
DR   KEGG; xcc:XCC4067; -.
DR   PATRIC; fig|190485.4.peg.4359; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_0_6; -.
DR   OMA; EILVGWQ; -.
DR   BioCyc; MetaCyc:MON-21811; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..300
FT                   /note="2-keto-3-deoxy-L-fuconate dehydrogenase"
FT                   /id="PRO_0000419049"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         63..90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q3T046"
FT   BINDING         112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q3T046"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3T046"
FT   BINDING         205
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q3T046"
FT   BINDING         234..238
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q3T046"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3T046"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3T046"
SQ   SEQUENCE   300 AA;  31436 MW;  CE8D137977B21E3D CRC64;
     MAADRTAAGT AVRRRQCRGG VRRQRTHVLS SATAGGPHPR NLIGMTVSIP TTPNTRLQGK
     RCLITAAGAG IGRESALACA RAGAHVIATD IDAAALQALA AESDAITTQL LDVTDAAAIT
     ALVAAHGPFD VLFNCAGYVH QGSILDCDEP AWRRSFSINV DAMYYTCKAV LPGMLERGRG
     SIINMSSVAS SIKGVPNRFV YGVTKAAVIG LSKAIAADYV AQGVRCNAIC PGTIKTPSLG
     QRVQALGGDE QAVWKSFTDR QPMGRLGDPR EIAQLVVYLA SDESSFTTGQ THIIDGGWSN