ID A5FYW4_ACICJ Unreviewed; 342 AA.
AC A5FYW4;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:ABQ30796.1};
GN OrderedLocusNames=Acry_1590 {ECO:0000313|EMBL:ABQ30796.1};
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ30796.1, ECO:0000313|Proteomes:UP000000245};
RN [1] {ECO:0000313|EMBL:ABQ30796.1, ECO:0000313|Proteomes:UP000000245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ30796.1,
RC ECO:0000313|Proteomes:UP000000245};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
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DR EMBL; CP000697; ABQ30796.1; -; Genomic_DNA.
DR RefSeq; WP_011942355.1; NC_009484.1.
DR AlphaFoldDB; A5FYW4; -.
DR STRING; 349163.Acry_1590; -.
DR KEGG; acr:Acry_1590; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_5_5; -.
DR Proteomes; UP000000245; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd08232; idonate-5-DH; 1.
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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000245};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 24..137
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 178..303
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 342 AA; 34946 MW; 6CCE0B78634B69D9 CRC64;
MTAIVIHAAG DLRIEDRPAP PPGPDEVRVR VRRGGICGSD LHYMRHGGFG PVRLAEPMVL
GHEVAGEVED AGAETGFAPG EAVAIDPSLP CGACRFCAAG ATQHCTDMRF FGSAMRRPHV
HGAFRSAITV PARQLVRLPA GLAVERAAFA EPLAVGLHAA TRAGIGPGMR VIIAGMGPIG
LLALLAAWHR GAAEIVACDV LGAPLALAAR LGATETVDLG REPDGLARFA GGKGWFDAGI
EASGAASSLA GLIGVVRPQG RIAQLGLGGD MSLPLMALVS KEIELAGAFR FGPEFAEAVA
LLASGAIDPD PLLSAVLPAE RAAEAFALAA DKARAVKVQL AF
//