ID I4F1A4_9ACTN Unreviewed; 348 AA.
AC I4F1A4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:CCH89417.1};
GN OrderedLocusNames=MODMU_4015 {ECO:0000313|EMBL:CCH89417.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH89417.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH89417.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH89417.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
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; FO203431; CCH89417.1; -; Genomic_DNA.
DR RefSeq; WP_014741994.1; NC_017955.1.
DR AlphaFoldDB; I4F1A4; -.
DR STRING; 477641.MODMU_4015; -.
DR KEGG; mmar:MODMU_4015; -.
DR PATRIC; fig|477641.3.peg.3760; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_11; -.
DR OMA; MRATTIH; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 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:UP000006461};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..127
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 181..306
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 348 AA; 35536 MW; 459D672641E065DF CRC64;
MRAAVHQAAG TITVEDVPDA ALVEPTDAVV RVLRSCICGS DLWSYRGIID RAAGSRTGHE
FIGVVTDVGA AVGTVRPGDL VVAPFAWSDN TCPACQDGVH TRCDNGGGFG APGSDGGQGE
AVRVPQADGT LVAVPGGPDG VDDALLPALL TLSDVMATGL HGAVLAGVEE GSTVAVIGDG
AVGLCAVLGA RAVLGAERVV LMSRHEDRAA LGRTFGATDV VAERGEEGIA AVRELTGGRG
VRHVVEAVGT PQSWEMALGM ARVGGRVGAV GVPHTSPEIP LFPIVRNHLT VSAGIAPVRK
YLPDLIERVM DGRLDPGAVF DLTLPLAQVA DGYAAMDERR SIKTMLAG
//
