ID C3YUQ9_BRAFL Unreviewed; 334 AA.
AC C3YUQ9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase {ECO:0000256|ARBA:ARBA00040603};
DE EC=1.1.1.179 {ECO:0000256|ARBA:ARBA00038984};
DE EC=1.3.1.20 {ECO:0000256|ARBA:ARBA00038853};
DE AltName: Full=D-xylose 1-dehydrogenase {ECO:0000256|ARBA:ARBA00043025};
DE AltName: Full=D-xylose-NADP dehydrogenase {ECO:0000256|ARBA:ARBA00042988};
DE AltName: Full=Dimeric dihydrodiol dehydrogenase {ECO:0000256|ARBA:ARBA00042926};
GN ORFNames=BRAFLDRAFT_212150 {ECO:0000313|EMBL:EEN55960.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN55960.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN55960.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN55960.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,2R)-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol +
CC H(+) + NADPH; Xref=Rhea:RHEA:16729, ChEBI:CHEBI:10702,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18135, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.3.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00036133};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH;
CC Xref=Rhea:RHEA:22000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15867,
CC ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.179; Evidence={ECO:0000256|ARBA:ARBA00036678};
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC {ECO:0000256|ARBA:ARBA00010928}.
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DR EMBL; GG666554; EEN55960.1; -; Genomic_DNA.
DR RefSeq; XP_002599948.1; XM_002599902.1.
DR AlphaFoldDB; C3YUQ9; -.
DR STRING; 7739.C3YUQ9; -.
DR eggNOG; KOG2741; Eukaryota.
DR InParanoid; C3YUQ9; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR22604; OXIDOREDUCTASES; 1.
DR PANTHER; PTHR22604:SF105; TRANS-1,2-DIHYDROBENZENE-1,2-DIOL DEHYDROGENASE; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
FT DOMAIN 5..122
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
SQ SEQUENCE 334 AA; 36903 MW; 6A538BA4515141EE CRC64;
MAPTRWGFVS AGKISNDFKV ALDTLPKDEH QVVAVAARSL ESAQKFAKTH DIQRAYGSYA
ELAAQDDIDV VYIGSIHTQH APVTTMMLQA GKPVLCEKPM SVNSREAWQM IGLAKEKNLF
FMEAVWSRFF PAYKKIRDII DSGAVGEVKV VTACFGFNVG DVPRLRERSQ GGGSLLDLGI
YPLQFATMSV RRGRTTGCHL LMMFFPTEVD ETVTVVLKYS GNRMATLLCS MSANLANEAY
VYGTKASLKI PNFWCPTEVI APDGTHQFPL PPPGKPLNFN NSTGMRFEAI EVRRCLQEGL
IESPLMTHAM SLQIAGILDQ ARKVVGVVYD QDKE
//