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Database: UniProt
Entry: U1LQA1_9MICO
LinkDB: U1LQA1_9MICO
Original site: U1LQA1_9MICO 
ID   U1LQA1_9MICO            Unreviewed;       390 AA.
AC   U1LQA1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Molecular chaperone GroES {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L332_07050 {ECO:0000313|EMBL:ERG64207.1};
OS   Agrococcus pavilionensis RW1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agrococcus.
OX   NCBI_TaxID=1330458 {ECO:0000313|EMBL:ERG64207.1, ECO:0000313|Proteomes:UP000016462};
RN   [1] {ECO:0000313|EMBL:ERG64207.1, ECO:0000313|Proteomes:UP000016462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RW1 {ECO:0000313|EMBL:ERG64207.1,
RC   ECO:0000313|Proteomes:UP000016462};
RX   PubMed=23814108;
RA   White R.A.III., Grassa C.J., Suttle C.A.;
RT   "First draft genome sequence from a member of the genus agrococcus,
RT   isolated from modern microbialites.";
RL   Genome Announc. 1:e00391-13(2013).
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:ERG64207.1}.
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DR   EMBL; ASHR01000025; ERG64207.1; -; Genomic_DNA.
DR   RefSeq; WP_021010633.1; NZ_ASHR01000025.1.
DR   AlphaFoldDB; U1LQA1; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000016462; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016462};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          26..140
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          189..253
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   390 AA;  41945 MW;  571126064DEEB072 CRC64;
     MRALTWQGKR KVSVEEVPDP VIQEPTDAVI RITSTAICGS DLHLYELFAP FLKKGDILGH
     EPMGIVEEVG SAVADLQVGD RVVIPFVVAC GSCFMCRKGL TTQCETTQNR HSGTGASLYG
     YTSLYGSVPG GQAERLRVPY ADFNATKVGS ELADDRYLFL SDILPTAWQG VAYAGLEPGQ
     TLGVMGLGPV GQFVARIGKH LGHRVIAVEP VAERRAMAER YGVETLDMPD ATDALKDLTD
     GRGPDAIVDA VGMEAHGAPG AATAQQLVGA LPDLLAKPMM RHAGLDRLSA LHTAFDAVRR
     GGTVSLSGVY VGSADPMPMM TLFDKQITLR MGQCNVQSWR DELLPLVEDP ADPLGTGDLT
     THLVPLEQAP EYYEIFQKKE DDCIKVVLQP
//
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