ID C3ZG10_BRAFL Unreviewed; 306 AA.
AC C3ZG10;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 65.
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_57457 {ECO:0000313|EMBL:EEN48485.1};
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:EEN48485.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN48485.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN48485.1};
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; GG666616; EEN48485.1; -; Genomic_DNA.
DR RefSeq; XP_002592474.1; XM_002592428.1.
DR AlphaFoldDB; C3ZG10; -.
DR STRING; 7739.C3ZG10; -.
DR eggNOG; KOG2741; Eukaryota.
DR InParanoid; C3ZG10; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
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 Pfam; PF02894; GFO_IDH_MocA_C; 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"
FT DOMAIN 137..249
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 306 AA; 33987 MW; F6B7BD0EEA234664 CRC64;
MAPTRWGIVG AGKISNDFKV ALDTLPAEEH QVVAVAARSL ERAQEFATTH TIPSAYGSYA
ELAAQKFIDV VYIGVKEPQH ATVTTMMLQS GKPVLCEKPK STDSREVQQM ISLAKEKNLF
FMEAIWSRFF PVYEKVREIL RSGELGEVRM VTASFGINFD GVPRLKDRSL AVGSLIEAGI
YPIQFATMVF GEEKPQGGTA TGHLTDTGVD ESATVVLKYS NNRMAVLTCS VSTTLSQEAY
IYGTMGSLKV PNFWCPTELI TPTRSHYFPL LTPEKPLNYF NSTGLRYEAM EVRRCLQNGQ
KMFLLK
//