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Database: UniProt
Entry: A0A0S9R8F0_9ACTN
LinkDB: A0A0S9R8F0_9ACTN
Original site: A0A0S9R8F0_9ACTN 
ID   A0A0S9R8F0_9ACTN        Unreviewed;       394 AA.
AC   A0A0S9R8F0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Molecular chaperone GroES {ECO:0000313|EMBL:KQP78393.1};
GN   ORFNames=ASF37_07460 {ECO:0000313|EMBL:KQP78393.1};
OS   Aeromicrobium sp. Leaf289.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP78393.1, ECO:0000313|Proteomes:UP000051640};
RN   [1] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQP78393.1}.
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DR   EMBL; LMNK01000002; KQP78393.1; -; Genomic_DNA.
DR   RefSeq; WP_056556417.1; NZ_LMNK01000002.1.
DR   AlphaFoldDB; A0A0S9R8F0; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000051640; Unassembled WGS sequence.
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|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          25..141
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          189..267
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   394 AA;  42632 MW;  B08BE5C0D856451B CRC64;
     MRAVTWQGRR DIQVHDVPDP RIEDPGDVVL KVTRTGLCGS DLHLYEVMGP FMNTGDVLGH
     ETMGEVVEVG AGITNLAVGD RVVVPFQIAC GDCFMCRKGL QTQCETTQVR SHGTGAALFG
     YSELYGSVPG GQAEYLRVPH ADYGAIKVGP DLPDERYVYL SDVMPTAWQA VRYADVHEGD
     TLAVVGLGPI GDMAARLALH QGIRVIGIDL VPERLERARQ RGVETLHVED DDVVETVFEL
     TSGRGADGVI DAVGMEAHGS PAPSVLQKAV GLLPDGLAKQ AMTSASVDRL AALHLSTQLV
     RRGGTVSLSG VYTGTHDPMP MQQLFDRQVT LRMGQANVKR WVDDLMPLAE RADDPLGLES
     FATHRLSLED APRAYDIFQR KDDGAVKVVF DPSL
//
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