ID A0A084VNK1_ANOSI Unreviewed; 315 AA.
AC A0A084VNK1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=AGAP009611-PA-like protein {ECO:0000313|EMBL:KFB39545.1};
GN ORFNames=ZHAS_00006889 {ECO:0000313|EMBL:KFB39545.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB39545.1};
RN [1] {ECO:0000313|EMBL:KFB39545.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC006889-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; ATLV01014759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE524984; KFB39545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084VNK1; -.
DR STRING; 74873.A0A084VNK1; -.
DR EnsemblMetazoa; ASIC006889-RA; ASIC006889-PA; ASIC006889.
DR VEuPathDB; VectorBase:ASIC006889; -.
DR VEuPathDB; VectorBase:ASIS016630; -.
DR OMA; CVDLEAC; -.
DR Proteomes; UP000030765; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765}.
FT DOMAIN 6..306
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 131..277
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 315 AA; 34433 MW; 95BC17192225D92A CRC64;
MRRPKVLVTH RQVQPVALER LQRECDVILP DVDFPTRANI LDLCPGIDGL LWTSYKMKLD
RDILQATGPN LKAVSLTMNG VDCVDLDELA TRNIPLGHTP HIPNGAVADL AIGLMIAASN
AIFSSREPDA HPCIQGSTVG IVGFGGIGEL IAKRLQGFDV ENFLYCGHSV KENAKKFNAQ
FVTREELLRR SDYVFIACPL TPDTLRMFNR DTFSIMKPTA VLVNVARGAI VDEGALVNAL
KSGKIRAAAL DTVTTEPIPA DSELFQLSNC VIIPHLGTAT KKTRDQMALR AVDNLLAGMR
GEAMPSQYFK RKTAN
//
