ID S9RN28_9RHOB Unreviewed; 567 AA.
AC S9RN28;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EPX79500.1};
DE EC=1.1.1.1 {ECO:0000313|EMBL:EPX79500.1};
GN ORFNames=Salmuc_04613 {ECO:0000313|EMBL:EPX79500.1};
OS Salipiger mucosus DSM 16094.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX79500.1, ECO:0000313|Proteomes:UP000015347};
RN [1] {ECO:0000313|Proteomes:UP000015347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX PubMed=25197501; DOI=10.4056/sigs.4909790;
RA Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT clade.";
RL Stand. Genomic Sci. 9:1331-1343(2014).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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:EPX79500.1}.
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DR EMBL; APVH01000037; EPX79500.1; -; Genomic_DNA.
DR AlphaFoldDB; S9RN28; -.
DR STRING; 1123237.Salmuc_04613; -.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_480506_0_0_5; -.
DR Proteomes; UP000015347; Unassembled WGS sequence.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd14861; Fe-ADH-like; 1.
DR Gene3D; 3.40.50.1970; -; 2.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF102; ALCOHOL DEHYDROGENASE 4; 1.
DR Pfam; PF00465; Fe-ADH; 2.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 2.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EPX79500.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015347}.
FT DOMAIN 10..122
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT DOMAIN 138..375
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT REGION 367..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 61563 MW; 5174865425B26597 CRC64;
MSLIANWSYP TAVRFGAGRI SELAEACKAA GMSKPLLVTD KGLADLPITK QALDILKAAG
LEADLFAEVD PNPNERNLGA GVVAFKQGRH DGVVAFGGGS GLDLGKCVAF MAGQTRPVWD
FEDIGDWCMS LIANWSYPTA VRFGAGRISE LAEACKAAGM SKPLLVTDKG LADLPITKQA
LDILKAAGLE ADLFAEVDPN PNERNLGAGV VAFKQGRHDG VVAFGGGSGL DLGKCVAFMA
GQTRPVWDFE DIGDWWTRAD ASAIAPIVAV PTTAGTGSEV GRAGVLTNSE THEKKIIFHP
KMLPATVICD PELTVGMPKA ITAGTGLDAF AHCVEAFSSP HYHPMSQGIA LEGMRLVVEN
LPRAFEQPDD IEARAPHDER RRHGRHRLPE GAGRDPRAEP PGRRAFPHPP RHDQRGLHAR
GAGVQRPRDR RPFRQGDGLP RYRGRFRRFP RLCRRTERTA RRAEGPRRAR RDRGEHPHAG
QGRDHRPLLR RQPGQADRGE PHAALPRGDV GTRANLDVTK AAPIPGAAFP FAMPVSRHRR
HPEQRAALTP GPAERRLRLR PRRAARC
//
