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Database: UniProt
Entry: E1J6J2_ECOLX
LinkDB: E1J6J2_ECOLX
Original site: E1J6J2_ECOLX 
ID   E1J6J2_ECOLX            Unreviewed;       358 AA.
AC   E1J6J2;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=GroES-like protein {ECO:0000313|EMBL:EFK68487.1};
GN   ORFNames=HMPREF9347_02530 {ECO:0000313|EMBL:EFK68487.1};
OS   Escherichia coli MS 124-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=679205 {ECO:0000313|EMBL:EFK68487.1, ECO:0000313|Proteomes:UP000003390};
RN   [1] {ECO:0000313|EMBL:EFK68487.1, ECO:0000313|Proteomes:UP000003390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS 124-1 {ECO:0000313|EMBL:EFK68487.1,
RC   ECO:0000313|Proteomes:UP000003390};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={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:EFK68487.1}.
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DR   EMBL; ADWT01000018; EFK68487.1; -; Genomic_DNA.
DR   RefSeq; WP_000645203.1; NZ_ADWT01000018.1.
DR   AlphaFoldDB; E1J6J2; -.
DR   SMR; E1J6J2; -.
DR   GeneID; 75203082; -.
DR   Proteomes; UP000003390; 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; cd08258; Zn_ADH4; 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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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          26..132
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          185..316
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   358 AA;  38714 MW;  26D92736F7CD9562 CRC64;
     MKALARFGKA FGGYKMIDVP QPICGPEDVV IEIKAAAICG ADMKHYNVDS GSDEFNSIRG
     HEFAGCIAQV GEKVKDWKVG QRVVSDNSGH VCGVCPACEQ GDFLCCTEKV NLGLDNNTWG
     GGFSKYCLVP GEILKIHRHA LWEIPDGVDY EDAAVLDPIC NAYKSIAQQS KFLPGQDVVV
     IGTGPLGLFS VQMARIMGAV NIVVVGLQED VAVRFPVAKE LGATAVVNGS TEDVVARCQQ
     ICGKDNLGLV IECSGANIAL KQAIEMLRPN GEVVRVGMGF KPLDFSINDI TAWNKSIIGH
     MAYDSTSWRN AIRLLASGAI KVKPMITHRI GLSQWREGFD AMVDKTAIKV IMTYDFDE
//
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