ID   A0A1G9SUK2_9FIRM        Unreviewed;       364 AA.
AC   A0A1G9SUK2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=L-iditol 2-dehydrogenase {ECO:0000313|EMBL:SDM39149.1};
GN   ORFNames=SAMN04488502_104122 {ECO:0000313|EMBL:SDM39149.1};
OS   Dendrosporobacter quercicolus.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Dendrosporobacter.
OX   NCBI_TaxID=146817 {ECO:0000313|EMBL:SDM39149.1, ECO:0000313|Proteomes:UP000214880};
RN   [1] {ECO:0000313|EMBL:SDM39149.1, ECO:0000313|Proteomes:UP000214880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1736 {ECO:0000313|EMBL:SDM39149.1,
RC   ECO:0000313|Proteomes:UP000214880};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={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; FNHB01000004; SDM39149.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9SUK2; -.
DR   STRING; 146817.SAMN04488502_104122; -.
DR   OrthoDB; 1674659at2; -.
DR   Proteomes; UP000214880; 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:UP000214880};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          24..128
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          176..305
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   364 AA;  38536 MW;  CEC554EB5E58D7EE CRC64;
     MKAAVYKGIE EIEIEELEKP GLTPGSILLK VKACAICGGD LRTFRHGHAA IKPPIVLGHE
     TAGEIVETAP EVKNFRAGDR VIVAPGIGCN HCSYCSSGWQ NMCYTRTTIA HHYNGGFAEY
     LLIPAGAVTA GNINRIPDEV TYLEASLAEP LACVLNGQEV MNIGLGDSVA VIGAGPIGCM
     HAEVARARGA GKVILINRSA RRLEEARKFG YDAYVDLSAT DGIEAVMELT GGLGANVVIV
     TAGTHEAQNL GIAMAGKMGK VCLFAGLPKS QPSIAFDVNH VHYRQITVYG AFSSAPRHNA
     LALELIRSGK VSAKKLLTHV VSLDKIKTGL DLVNERAGLR VTVSPFIDEL TEEIAGHPGV
     IVVK
//