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Database: UniProt
Entry: G0I730_STRES
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ID   G0I730_STRES            Unreviewed;       345 AA.
AC   G0I730;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=Zinc-containing alcohol dehydrogenase {ECO:0000313|EMBL:AEL11316.1};
GN   OrderedLocusNames=SPPN_09525 {ECO:0000313|EMBL:AEL11316.1};
OS   Streptococcus pseudopneumoniae (strain IS7493).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1054460 {ECO:0000313|EMBL:AEL11316.1, ECO:0000313|Proteomes:UP000001637};
RN   [1] {ECO:0000313|EMBL:AEL11316.1, ECO:0000313|Proteomes:UP000001637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IS7493 {ECO:0000313|EMBL:AEL11316.1,
RC   ECO:0000313|Proteomes:UP000001637};
RX   PubMed=21994930; DOI=10.1128/JB.06075-11;
RA   Shahinas D., Tamber G.S., Arya G., Wong A., Lau R., Jamieson F., Ma J.H.,
RA   Alexander D.C., Low D.E., Pillai D.R.;
RT   "Whole-genome sequence of Streptococcus pseudopneumoniae isolate IS7493.";
RL   J. Bacteriol. 193:6102-6103(2011).
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; CP002925; AEL11316.1; -; Genomic_DNA.
DR   RefSeq; WP_000833733.1; NC_015875.1.
DR   AlphaFoldDB; G0I730; -.
DR   GeneID; 45219095; -.
DR   KEGG; std:SPPN_09525; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_3_9; -.
DR   OMA; CCRNFGT; -.
DR   Proteomes; UP000001637; 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; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          26..123
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          179..288
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   345 AA;  36764 MW;  EB75995A1FF5A63F CRC64;
     MKSAVYTKAG QVGLASIERP QIIEADDVII RVVRACVCGS DLWRYRNPET KAGHKNSGHE
     AIGIVEEAGE AITTVKPGDF VIVPFTHGCG ECDACLAGFD GSCDNHIGNN LGGDFQAEYI
     RFHYANWALV KIPGQPSDYT EGMLKSLLTL ADVMPTGYHA ARVANVQKGD KVVVIGDGAV
     GQCAVIAAKM RGASQIILMS RHEDRQKMAM ESGATAVVAE RGQEGITKVR EILGGGADAA
     LECVGTEAAI EQALGVLHNG GRMGFVGVPH YNNRALGSTF IQNISVAGGA ASATTYDKQF
     LLKAVLDGDI NPGRVFTSSY KLEDIDQAYK DMDERKTIKS MIVIE
//
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