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Database: UniProt
Entry: F4W7M8_ACREC
LinkDB: F4W7M8_ACREC
Original site: F4W7M8_ACREC 
ID   F4W7M8_ACREC            Unreviewed;       332 AA.
AC   F4W7M8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=G5I_01444 {ECO:0000313|EMBL:EGI69901.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI69901.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; GL887844; EGI69901.1; -; Genomic_DNA.
DR   RefSeq; XP_011067844.1; XM_011069542.1.
DR   RefSeq; XP_011067845.1; XM_011069543.1.
DR   AlphaFoldDB; F4W7M8; -.
DR   STRING; 103372.F4W7M8; -.
DR   EnsemblMetazoa; XM_011069542.1; XP_011067844.1; LOC105154186.
DR   EnsemblMetazoa; XM_011069543.1; XP_011067845.1; LOC105154186.
DR   GeneID; 105154186; -.
DR   KEGG; aec:105154186; -.
DR   eggNOG; KOG2741; Eukaryota.
DR   InParanoid; F4W7M8; -.
DR   OrthoDB; 2898964at2759; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
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;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755}.
FT   DOMAIN          5..122
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
SQ   SEQUENCE   332 AA;  36899 MW;  0589ACF12196ACD9 CRC64;
     MVTLRWGIAS AGKISHDFVT ALQSLPADEH NVIAVAARQL SRAKDFAKLH EIKTVYDDYE
     KLGLNKDIDI VYIGAIHPQH FDIAMLMLKH GKHVLCEKPL TMNLKQTTEL INYAKSKNLF
     LMEAVWSRCF PVYDIVRKEI ASGNIGDIHQ VIVSFGFQML DVDRITLKEL GGGSILDLGI
     YCLQFACLVY NNEMPESIKA AGILNKNGVD MSMSATLIYK GNRTATITTN ALVDLPNEAY
     ICGTKGMIKV PSFWCPTKVE LPSGTVQTSL PKLKHEVNYI NSAGLSYEAV EARNCILKGL
     IESPKISHDT SLLLAKLEDE LRRQLGVVYL QD
//
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