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Database: UniProt
Entry: A0A1I1BUE9_9PSEU
LinkDB: A0A1I1BUE9_9PSEU
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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}.
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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
//
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