ID C3ZC66_BRAFL Unreviewed; 299 AA.
AC C3ZC66;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Aldo-keto reductase family 1 member A1-A-like {ECO:0000313|RefSeq:XP_035663736.1};
GN Name=LOC118407376 {ECO:0000313|RefSeq:XP_035663736.1};
GN ORFNames=BRAFLDRAFT_214894 {ECO:0000313|EMBL:EEN49838.1};
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:EEN49838.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN49838.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN49838.1};
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).
RN [2] {ECO:0000313|RefSeq:XP_035663736.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035663736.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035663736.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC {ECO:0000256|ARBA:ARBA00007905}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG666606; EEN49838.1; -; Genomic_DNA.
DR RefSeq; XP_002593827.1; XM_002593781.1.
DR RefSeq; XP_035663736.1; XM_035807843.1.
DR STRING; 7739.C3ZC66; -.
DR KEGG; bfo:118407376; -.
DR eggNOG; KOG1577; Eukaryota.
DR InParanoid; C3ZC66; -.
DR OMA; WQSKENE; -.
DR OrthoDB; 890110at2759; -.
DR Proteomes; UP000001554; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 1.
DR PANTHER; PTHR11732:SF507; ALDO_KET_RED DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001554}.
FT DOMAIN 17..289
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 50
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 78
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 299 AA; 33668 MW; 4D6DC45DCA1942BC CRC64;
MTCPTVKLST GASMPLVGLG TWQSKNNECY EAVKAALDAG YRHIDTAELY QNEKEIGRAL
KEKMDAGMKR EEVFVVSKLW NTRHHPDDVL PACQKSLDDL GLEYLDLYLM HHPFPWARGD
NLLPINADGK AEHSDVHFMD TWKEMEKLVD AGLVKAIGVS NFNISQMEEV LTNGRINPAV
NQVESHPYVT CNRMLEFCTE KGVVMTAYCP LGAPGDLKDH GLAVLEDSEL KKIAEKHGKT
PAQVCLRWQV QRGVVVIPKS LRAARMVENS QIFDFELSAG DVEIINNLNR DGRVYKWEW
//