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Database: UniProt
Entry: A0A1L9RV17_ASPWE
LinkDB: A0A1L9RV17_ASPWE
Original site: A0A1L9RV17_ASPWE 
ID   A0A1L9RV17_ASPWE        Unreviewed;       404 AA.
AC   A0A1L9RV17;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Opine dehydrogenase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASPWEDRAFT_735324 {ECO:0000313|EMBL:OJJ38718.1};
OS   Aspergillus wentii DTO 134E9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Cremei.
OX   NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ38718.1, ECO:0000313|Proteomes:UP000184383};
RN   [1] {ECO:0000313|Proteomes:UP000184383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:57945; EC=1.1.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001662};
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DR   EMBL; KV878210; OJJ38718.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9RV17; -.
DR   VEuPathDB; FungiDB:ASPWEDRAFT_735324; -.
DR   OrthoDB; 2230586at2759; -.
DR   Proteomes; UP000184383; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003421; Opine_DH.
DR   PANTHER; PTHR38015; BLR6086 PROTEIN; 1.
DR   PANTHER; PTHR38015:SF1; OCTOPINE_DH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   Pfam; PF02317; Octopine_DH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184383}.
FT   DOMAIN          10..110
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          192..340
FT                   /note="Opine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF02317"
SQ   SEQUENCE   404 AA;  44182 MW;  8835EE6442479E41 CRC64;
     MASHIEPSSV TIVGAGPCGC AFAADLASRG KSVMLYGHPD HRGAIPMIEK NGGWLTASGE
     VSGDYQIQTT SDLYLAIRHS SFIVTTVPSY GQDDILTVLS QFDLRNHTLI INVGNFFYLS
     ARQKVNAYAI LETDISPYAT RITGDQVFVK GCKKSLAIWA EPPTTQIERH NHQAELALRR
     QVESIFSQNL VWCQSLLQVG LNNINPVVHC PAALMNAGWI EATKGDFYFY AQGMSPAVSR
     VTEKVDAERM AIGRAYGFDL VDVTTYMNQN YTHDQAYGNY HDFASTSVVH NKTKSAPTSM
     KHRYLLEDIL YGMVPWYELG LKCGLPSPTI RSLIEMASVV SGFDYLEHGR SLRSAGLGEA
     TKEQVLMALG GPVNDAPAVL APLSDAHLNT LESHAPLQKP QVAA
//
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