ID   A0A182F2P3_ANOAL        Unreviewed;       651 AA.
AC   A0A182F2P3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:AALB000725-PA};
OS   Anopheles albimanus (New world malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB000725-PA, ECO:0000313|Proteomes:UP000069272};
RN   [1] {ECO:0000313|EnsemblMetazoa:AALB000725-PA}
RP   IDENTIFICATION.
RC   STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB000725-PA};
RG   EnsemblMetazoa;
RL   Submitted (AUG-2022) to UniProtKB.
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   AlphaFoldDB; A0A182F2P3; -.
DR   STRING; 7167.A0A182F2P3; -.
DR   EnsemblMetazoa; AALB000725-RA; AALB000725-PA; AALB000725.
DR   VEuPathDB; VectorBase:AALB000725; -.
DR   VEuPathDB; VectorBase:AALB20_035301; -.
DR   Proteomes; UP000069272; Chromosome 2L.
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; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 4.
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; 2.
DR   Pfam; PF02826; 2-Hacid_dh_C; 2.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          20..318
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          115..292
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   DOMAIN          350..645
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          441..618
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   651 AA;  70014 MW;  B13C195CCFB52BBA CRC64;
     MANNGSRPVV LVTNMETPLK GIQKLQQKCD VIFPSTHPAT REEILELAGQ VDGIMWVGHM
     ALNGEVLDRG GSRLKAISTM SAGMDYVDVE EFKRRKFPLG YTPIVLNDAV ADTAVGLMIA
     ASRRFHEGRL AIDNSQWIGG PQWMLGRDIK GSTVGIIGFG GIGQTVARRL KGFEIGQLLY
     SGRRPKPEAE ALGAKLVPQS ELLQESDYVV LAVPLTNQTY HMINESTLSL MKSTAVLVNV
     ARGDLVDQKA LVAALKNGTI FAAGLDVVSP EPLPADDELL KLPNAVVIPH LGSATVQTRD
     NMAEIAALNV LSGIAGAPMM LRKPQIEQYS FGAKRPKLLV TCSDMPGSYV DRLREKCDVT
     VCSGTNRAEI LRSVSGADGI LWLTADRLDG EVLDAAGTQL AVVSTMTSGM DYVDADEFAR
     RRIALGHTPT VVNGPVADIA IGLMLAAARR FHEGRQKIAA GQWEMRPQWM LGQDVPGSTI
     GIVGFGGIGQ TIRKRLQGFD IARCLYTGRS RKPEADLTGA EFVELPTLLR ESDFVFIACP
     LTTETANMIN RETLAIMKPS SVLINVARGG IVDQPALVEA LRNGTIFAAG LDVMSPEPLD
     PKDPLLTLPN CIVVPHLGTA TQRSLLDMFT ITANNVLSVL AGGQPVAPYR K
//