ID   A1R5V3_PAEAT            Unreviewed;       382 AA.
AC   A1R5V3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   SubName: Full=Putative alcohol dehydrogenase {ECO:0000313|EMBL:ABM07096.1};
GN   OrderedLocusNames=AAur_1866 {ECO:0000313|EMBL:ABM07096.1};
OS   Paenarthrobacter aurescens (strain TC1).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Paenarthrobacter.
OX   NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM07096.1, ECO:0000313|Proteomes:UP000000637};
RN   [1] {ECO:0000313|EMBL:ABM07096.1, ECO:0000313|Proteomes:UP000000637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1 {ECO:0000313|EMBL:ABM07096.1,
RC   ECO:0000313|Proteomes:UP000000637};
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.,
RA   Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT   aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
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; CP000474; ABM07096.1; -; Genomic_DNA.
DR   RefSeq; WP_011774559.1; NC_008711.1.
DR   AlphaFoldDB; A1R5V3; -.
DR   STRING; 290340.AAur_1866; -.
DR   KEGG; aau:AAur_1866; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_3_11; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000000637; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08283; FDH_like_1; 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; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          25..140
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          188..259
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   382 AA;  41577 MW;  634CEE0E779FE520 CRC64;
     MRSMVYRGPY KVRVEEKDIP QIEHPNDAIV QVKLGAICGS DLHLYHGMMP DTRVGMTFGH
     EFVGVVHEVG SSVQNLEVGD RVMVPFNIYC GSCYFCSRGL YSNCHNVNPN ATAVGGIYGY
     SHTCGGYDGG QAEFVRVPFA DVGPTTIPDW MDEEDAVLLT DALPTGYFGA QLGDIAEGDT
     VVVFGAGPVG LFAAKSAWLM GAGRVIVIDH LEYRLEKARS FAHAETYNFV EYDDIVVHLK
     KATDYLGADV VIDAVGAEAD GNFLQHVTSS KLKLQGGSPI ALNWAIDSVR KGGTVSVVGA
     YGPLFSAVKF GDAMNKGLTL RMNQCPVKRQ WPRLFEHIRN GHLKPSDIVT HRIPLEHIAE
     GYHIFSAKLD DCIKPLIVAT SA
//