ID J2JSH8_9ACTN Unreviewed; 364 AA.
AC J2JSH8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Alcohol dehydrogenase catalytic domain-containing protein {ECO:0000313|EMBL:QTZ90861.1};
DE SubName: Full=L-iditol 2-dehydrogenase {ECO:0000313|EMBL:EJJ03343.1};
GN ORFNames=SU9_004765 {ECO:0000313|EMBL:QTZ90861.1}, SU9_29381
GN {ECO:0000313|EMBL:EJJ03343.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ03343.1};
RN [1] {ECO:0000313|EMBL:EJJ03343.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ03343.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ90861.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ90861.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) 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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; AJGV01000185; EJJ03343.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ90861.1; -; Genomic_DNA.
DR RefSeq; WP_006607381.1; NZ_CP072931.1.
DR AlphaFoldDB; J2JSH8; -.
DR STRING; 1160718.SU9_29381; -.
DR KEGG; sauh:SU9_004765; -.
DR PATRIC; fig|1160718.3.peg.5944; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_11; -.
DR OrthoDB; 9797931at2; -.
DR Proteomes; UP000009036; Chromosome.
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; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR43161; SORBITOL 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:UP000009036};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 31..139
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 179..304
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 364 AA; 38037 MW; 243D0E03AC6B0023 CRC64;
MDSDTMMQAL VFETGERLRL CSRPLPALRH PDDVLVRVAA SGICGTDRSI VLGDFPARSG
VVLGHEAAGG VVATGPAVGS LAPGGRVVIN PTYHCGSCRC CRRGMAAHCA SKDGREIGVD
RDGTLAEYVV VPAPFLHPLP PGVSYRRAAL VEPLACVLNN LTAAALRWTD RCLVLGAGPI
GTLCALVLAF RGHRVTVVER DAVRVELAQH VLPAPTQVVP AREGDLWPAA GGWEAGPDVV
VDTTGVLLAD ALEVVATGGT VVAMGERETA TATIPVRSLV TRGVRLVGAG PYPPHLFQTA
LDLARDLPLD SLVTHTLPLH RYAEAFAALH VPLADTGPAP SSYAAMKVLL LPGDQAREES
RCAG
//
