ID A0A0S3TBP3_PHAAN Unreviewed; 376 AA.
AC A0A0S3TBP3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Vigan.11G210000 {ECO:0000313|EMBL:BAU02551.1};
GN ORFNames=VIGAN_11210000 {ECO:0000313|EMBL:BAU02551.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAU02551.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAU02551.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; AP015044; BAU02551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3TBP3; -.
DR Proteomes; UP000291084; Chromosome 11.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08301; alcohol_DH_plants; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF5; ALCOHOL DEHYDROGENASE-LIKE 6; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 36..123
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 203..333
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 376 AA; 40432 MW; 83EB6553166A5CB1 CRC64;
MAPSTSQVIT CKAAVAWGAG EPLVMEEVEV SPPQPMEIRI KVVSTSLCRS DLSAWESHAI
FPRIFGHEAS GIVESVGLGV TEFKEGDHVL TVFIGECMTC RQCTSGKSNV CQVLGLERRG
LMHSDQKTRF SIKGKPVYHY CAVSSFSEYT VIHSGCAVKV SPHAPLEKIC LLSCGVAAGL
GAAWNVADVS KGSTVVIFGL GTVGLSVAQA AKLRGASRII GVDNNPQKCE NAKAFGVTEV
VDPNSCEEPI AQVIKRITDG GADFSFECVG DTDMITTALQ SCCDGWGLTV TLGVPKAKPE
MSAHYGLLLM GRTLKGSLFG GWKPKSDLPS LVEKYVNKEI KIDDYITHNL PFDDINKAFN
LMKEGKCLRC VIHMQR
//
