ID B7LRA3_ESCF3 Unreviewed; 347 AA.
AC B7LRA3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Dehydrogenase, starvation-sensing protein with NAD(P)-binding and GroES domains {ECO:0000313|EMBL:CAQ89045.1};
GN Name=rspB {ECO:0000313|EMBL:CAQ89045.1};
GN OrderedLocusNames=EFER_1526 {ECO:0000313|EMBL:CAQ89045.1};
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ89045.1, ECO:0000313|Proteomes:UP000000745};
RN [1] {ECO:0000313|Proteomes:UP000000745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 /
RC JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73
RC {ECO:0000313|Proteomes:UP000000745};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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}.
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DR EMBL; CU928158; CAQ89045.1; -; Genomic_DNA.
DR AlphaFoldDB; B7LRA3; -.
DR KEGG; efe:EFER_1526; -.
DR HOGENOM; CLU_026673_11_0_6; -.
DR Proteomes; UP000000745; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08261; Zn_ADH7; 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 33..139
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 181..304
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 347 AA; 38213 MW; 0683D99C94551F98 CRC64;
MELVRKTMMV SVVVEKPGQM CLVESVKSEP KADEVCVKVE YAGICGSDLH IYHGANPFAV
YPRIVGHEFV GTIIQVGENI DPLRIGERVV VDPVISCGHC YPCSIGRPNV CESLNVLGVH
RDGGFTEYTC VPATNAYPVP EDIPANIAVT IEPYAVAANV TNRTGVYPTD IALVYGAGPA
GMTIIDVLRN VWQIPVIVVD QREDRLESAR RCGATYTFNN RNGSLREYLA SEKITPTLII
DAVCHPSILE EAVTLISSAG RIGLLGFSAT PSAIAQQELT RRELTLYSSR LNCRMFPTVI
EWMQHNLIHP ENIISHVFDI HHVDEAFKLI ESQQEGLCKV LLKFPES
//
