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Database: UniProt
Entry: E1VZ63_GLUAR
LinkDB: E1VZ63_GLUAR
Original site: E1VZ63_GLUAR 
ID   E1VZ63_GLUAR            Unreviewed;       365 AA.
AC   E1VZ63;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Putative Zn-dependent alcohol dehydrogenase {ECO:0000313|EMBL:CBT76916.1};
DE            EC=1.1.1.1 {ECO:0000313|EMBL:CBT76916.1};
GN   OrderedLocusNames=AARI_27050 {ECO:0000313|EMBL:CBT76916.1};
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:CBT76916.1, 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; CBT76916.1; -; Genomic_DNA.
DR   RefSeq; WP_013350030.1; NC_014550.1.
DR   AlphaFoldDB; E1VZ63; -.
DR   STRING; 861360.AARI_27050; -.
DR   KEGG; aai:AARI_27050; -.
DR   eggNOG; COG1062; Bacteria.
DR   HOGENOM; CLU_026673_14_1_11; -.
DR   OrthoDB; 334894at2; -.
DR   Proteomes; UP000006878; Chromosome.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43350:SF19; RIBULOSE-5-PHOSPHATE REDUCTASE; 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   ECO:0000313|EMBL:CBT76916.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006878};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          36..122
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          204..318
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   365 AA;  37588 MW;  A6A06C90ECB31B92 CRC64;
     MRQIQAAVLE HAQNQKPYAE HQPLVIRQLQ LEEPGPGEVL VRITAAGLCH SDLSVIDGNR
     PRPLPMVLGH ESAGIVEQVG RGVDLAIGQQ VISVFLPRCE KCDACATGGK LPCSAGSQSN
     AEGTLLGGAR RLFLDGTPVH HHLGVSAFAS HAVMDARSLI PVGADVPAPV AAVLGCAVLT
     GGGALRNAAK ATGDQDIAIV GLGGVGMAAL LVAAGQRTTG KILAIDANEE KLAIARELGA
     DDACTPQQAE GRTAQIVIEA AGHPRAFETA MQVSAVGSTV VTVGLPAPGA MSSIEPLALT
     AGARTVIGSY MGSALPARDI PCYEQLWCEG KLPLEKLVKT RALAEINQAL DELAEGRSVR
     QVLLA
//
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