GenomeNet

Database: UniProt
Entry: W5JAW6_ANODA
LinkDB: W5JAW6_ANODA
Original site: W5JAW6_ANODA 
ID   W5JAW6_ANODA            Unreviewed;       347 AA.
AC   W5JAW6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Glyoxylate/hydroxypyruvate reductase {ECO:0000313|EMBL:ETN61602.1};
GN   ORFNames=AND_006745 {ECO:0000313|EMBL:ETN61602.1};
OS   Anopheles darlingi (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN61602.1};
RN   [1] {ECO:0000313|EMBL:ETN61602.1, ECO:0000313|Proteomes:UP000000673}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA   Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT   "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT   the genome of the newly sequenced Anopheles darlingi.";
RL   BMC Genomics 11:529-529(2010).
RN   [2] {ECO:0000313|EMBL:ETN61602.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ETN61602.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23761445;
RA   Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA   Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA   Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA   Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA   de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA   Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA   Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA   Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA   Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA   de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA   Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA   Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA   Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA   Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA   Camargo E.P., de Vasconcelos A.T.;
RT   "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL   Nucleic Acids Res. 41:7387-7400(2013).
RN   [4] {ECO:0000313|EnsemblMetazoa:ADAC006745-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; ADMH02001646; ETN61602.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5JAW6; -.
DR   STRING; 43151.W5JAW6; -.
DR   EnsemblMetazoa; ADAC006745-RA; ADAC006745-PA; ADAC006745.
DR   VEuPathDB; VectorBase:ADAC006745; -.
DR   VEuPathDB; VectorBase:ADAR2_007580; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   HOGENOM; CLU_019796_1_2_1; -.
DR   OMA; RMMVEGH; -.
DR   OrthoDB; 6392at2759; -.
DR   Proteomes; UP000000673; 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   CDD; cd05301; GDH; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10996:SF119; FI03731P-RELATED; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719}; Pyruvate {ECO:0000313|EMBL:ETN61602.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000673}.
FT   DOMAIN          43..340
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          137..314
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   347 AA;  37483 MW;  BC82F4C035FCBFDC CRC64;
     MRTTIGRLLH YSVPRMLRKP QIEQYSFGAK RPKLLVTCSD IPGSYVDLLR EKCDVTVCSG
     TNRAEILRSV PGADGILWLT ADRLDGEVLD AAGSQLAVVS TMTSGMDYVD ADEFARRRIA
     LGHTPTVVNG AVADIAIGLM LAAARRFHEG RQKIATGQWE MRPQWMLGQD VPGSTIGIVG
     FGGIGQTIRK RLQGFDIARC LYTGRSRKPE ADLAGAEFVD LPTLLRESDF VFIACPLTSE
     TANMINRETL GIMKPSSVLI NVARGGIVDQ PALVKALRNG TIFAAGLDVM SPEPLDPEDP
     LLALPNCIVV PHLGTATQRS LLDMFTITAN NVLSVLAGGQ LVAPYKK
//
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