ID A0A1I1BUE9_9PSEU Unreviewed; 316 AA.
AC A0A1I1BUE9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=L-iditol 2-dehydrogenase {ECO:0000313|EMBL:SFB53767.1};
GN ORFNames=SAMN05216266_117103 {ECO:0000313|EMBL:SFB53767.1};
OS Amycolatopsis marina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=490629 {ECO:0000313|EMBL:SFB53767.1, ECO:0000313|Proteomes:UP000243799};
RN [1] {ECO:0000313|Proteomes:UP000243799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3568 {ECO:0000313|Proteomes:UP000243799};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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 EMBL; FOKG01000017; SFB53767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1BUE9; -.
DR STRING; 490629.SAMN05216266_117103; -.
DR Proteomes; UP000243799; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000243799};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 3..102
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 150..277
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 316 AA; 33070 MW; C9D8800088B24ACE CRC64;
MLHVGANTLC GTDLRILRGE KTRGVRFPSV LGHEFAGTVA AVGADVQGFA EGDKAAMCPV
IPCRRCVHCL HDRENVCANR RAMGYEYDGG LAEYVRIPAE AMAAGNLFPA DADIPLEQLA
LAEPLACTVN GHRRSGIRLG DVVLVIGAGP IGLLHLQLAR RAGASAVIVS EPSPSRRAVA
AKLGASHVVA PMELAATVEA LTDRTGVDAS IVCIGIPQLV NDAIALTRKA GNVNIFAGLP
ADGRVDIPAN EIHYKELVVT GTSAMHRRDY EQALRLIGNG EVDVASLVTD KMPLASVVEA
FELAQSGTGI KVAVVP
//