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Database: UniProt
Entry: E1W0C8_GLUAR
LinkDB: E1W0C8_GLUAR
Original site: E1W0C8_GLUAR 
ID   E1W0C8_GLUAR            Unreviewed;       390 AA.
AC   E1W0C8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Putative Zn-dependent alcohol dehydrogenase {ECO:0000313|EMBL:CBT77331.1};
DE            EC=1.1.1.- {ECO:0000313|EMBL:CBT77331.1};
GN   OrderedLocusNames=AARI_31300 {ECO:0000313|EMBL:CBT77331.1};
OS   Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS   JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Glutamicibacter.
OX   NCBI_TaxID=861360 {ECO:0000313|Proteomes:UP000006878};
RN   [1] {ECO:0000313|EMBL:CBT77331.1, ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RX   PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA   Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA   Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA   Vallaeys T.;
RT   "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT   adaptation to the surface of cheese.";
RL   PLoS ONE 5:E15489-E15489(2010).
RN   [2] {ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RA   Genoscope.;
RT   "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT   CIP 108037 / JCM 13566 / Re117).";
RL   Submitted (JUL-2010) 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|RuleBase:RU361277}.
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DR   EMBL; FQ311875; CBT77331.1; -; Genomic_DNA.
DR   RefSeq; WP_013350430.1; NC_014550.1.
DR   AlphaFoldDB; E1W0C8; -.
DR   STRING; 861360.AARI_31300; -.
DR   KEGG; aai:AARI_31300; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_3_11; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000006878; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CBT77331.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006878};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          25..141
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          189..254
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   390 AA;  42192 MW;  F8178DBEBE7AA7BD CRC64;
     MKALTWQGKR KIGYSDVPDP VIQDPGDIII KVTSTAICGS DLHLYELLGP YMHAGDVLGH
     ETMGIVQEIG SGITNLAVGD RVVIPFNISC GHCWMCEHGL QSQCETTQVR KHGKGAQFFG
     YSELYGQVPG GQAEYLRVPH ADYGAVKVGQ ELPDHRYLFL SDILPTAWQG VEYANVPENG
     TLAVYGLGPV GQLAARIGRY LGYEVLGIDP VAERRAMAER HGIKTLNFTK DTVGELRGRT
     GRGPDSVLDA VGMEAHGSPV SSMFQQATGL LPDKAAQLAM ENVSADRTSV LDSAIDAVRR
     GGTLSISGVY AGAATPMPML KLFDKQIQIR QGQCNVRSWT EHLLPLAEDP GDPLGLDDLV
     THEQPLSAGP QMYETFQKKQ DACIKVVLKP
//
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