ID   A0A183H3S2_9BILA        Unreviewed;       807 AA.
AC   A0A183H3S2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=2-Hacid_dh_C domain-containing protein {ECO:0000313|WBParaSite:OFLC_0000213101-mRNA-1};
GN   ORFNames=OFLC_LOCUS2132 {ECO:0000313|EMBL:VDO31979.1};
OS   Onchocerca flexuosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0000213101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:OFLC_0000213101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO31979.1, ECO:0000313|Proteomes:UP000267606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}.
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DR   EMBL; UZAJ01001166; VDO31979.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183H3S2; -.
DR   STRING; 387005.A0A183H3S2; -.
DR   WBParaSite; OFLC_0000213101-mRNA-1; OFLC_0000213101-mRNA-1; OFLC_0000213101.
DR   Proteomes; UP000050787; Unplaced.
DR   Proteomes; UP000267606; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          413..586
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   REGION          144..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   807 AA;  86430 MW;  E43DAC2E9F53C507 CRC64;
     MHEAVTTADQ RPPSMVFTAA ELPKFTTHPA TFIPTVFGGH VLVYESRSHP GHRREFAFKT
     RFTNQSGVSS CYYRCMSCRS MKNKVPPGPD GKPPQIPCIA VKNGFIVNDP DFPEANDHFC
     VPPTIDESRQ REANGFAKAI VKGRPRQKTT RKNNNNGNIG VIGNGSNAKK DSIIAAQLQA
     YQEMSNALLN GSVGNIFDIS SIAGGFDLSS DFSASSASQL LSLVTGGVKG ELDSAGDSSD
     FLKNIKIEDD DSDGTAKATH LLASLISSEP ALRTQMMLPT TAHRSNILSL PVATSTVATS
     SGSTEDEQLN GMNGPDIRSS PESSTAVIIN SLQGSDSRPP SVSSSSASLP LSGITVPTVL
     ANGLSANSRK RKGNGGNSLE AHFDEIFERY ILNNWEIVDN GKKPENIAEH TCALILALAR
     KIPQAVIAIK EGKWTRTEPY PEELFGKSLA IIGLGRIGLE IAIRMQVFGM RTFGYDPQVT
     QEEAARHGIR WLPLDQLWPQ ADYIVIHVPL IPRTKNLMCA STLARCRKGV KIINMGKAGI
     INEVDMLQAL NKGRVGGAAF DIYVEDAPVV RGLIEHPNVL CTPHTGTSPL QGHQRIANEI
     AENIISLNNS TGPYGAMNAA AATAALDEAK SQWIRAVATL TQTLAVIGNS PKAVTIRFPN
     SLVSLQKALH AGAVVGLMYA NGNIGSNLAT AEINARKEGV QIREEPCAAK ELIVVAGTRS
     VSGYPAPTGT VISAFNSCKV PVPLLASGTF IMDFADSHSF DIIDEDIKTK MMVEFSLLGG
     GRVGVLNDLT TDDVLELSKN YCLVKFD
//