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Database: UniProt
Entry: S5Y243_PARAH
LinkDB: S5Y243_PARAH
Original site: S5Y243_PARAH 
ID   S5Y243_PARAH            Unreviewed;       378 AA.
AC   S5Y243;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Iron-containing alcohol dehydrogenase {ECO:0000313|EMBL:AGT11522.1};
DE            EC=1.1.1.- {ECO:0000313|EMBL:AGT11522.1};
GN   ORFNames=JCM7686_pAMI8p021 {ECO:0000313|EMBL:AGT11522.1};
OS   Paracoccus aminophilus JCM 7686.
OG   Plasmid pAMI8 {ECO:0000313|EMBL:AGT11522.1,
OG   ECO:0000313|Proteomes:UP000015480}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT11522.1, ECO:0000313|Proteomes:UP000015480};
RN   [1] {ECO:0000313|EMBL:AGT11522.1, ECO:0000313|Proteomes:UP000015480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT11522.1};
RC   PLASMID=Plasmid pAMI8 {ECO:0000313|Proteomes:UP000015480};
RX   PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA   Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA   Schluter A., Puhler A., Bartosik D.;
RT   "Architecture and functions of a multipartite genome of the methylotrophic
RT   bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT   chromids.";
RL   BMC Genomics 15:124-124(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}.
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DR   EMBL; CP006655; AGT11522.1; -; Genomic_DNA.
DR   AlphaFoldDB; S5Y243; -.
DR   KEGG; pami:JCM7686_pAMI8p021; -.
DR   PATRIC; fig|1367847.3.peg.4503; -.
DR   HOGENOM; CLU_007207_0_0_5; -.
DR   Proteomes; UP000015480; Plasmid pAMI8.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08183; Fe-ADH-like; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
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; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR   PROSITE; PS00913; ADH_IRON_1; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AGT11522.1}; Plasmid {ECO:0000313|EMBL:AGT11522.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015480}.
FT   DOMAIN          10..369
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   378 AA;  38204 MW;  870CDD0A28894733 CRC64;
     MMPAFSVALP GQVLFGRGEA TKAPALTRSF GEKVLVVHGR DAARVGWLLA ELAGSEIRTM
     RCAAEPTLAM IEAALGELAG FRPDVVVGIG GGAVLDMAKA LAALIPAPGG PMDHLEVVGR
     GLPLALPALP VIALPTTAGT GAEATRNAVL GLPDHGRKVS LRDRGMLPRI AIVDPALTDD
     CPRGVTLASG LDALAQVIEP YVSNKATPFT DALTLPAIGR GLAALQSLMR GEDPAARDEM
     AWVSLTGGIA LANAGLGAVH GLAGVIGGMT TAAHGAVCGA LLGPVIAANR AKATGKIAAR
     LDTVCDILAA GLGVSADDAP RALITWAREA GLPGLQAHGL LPESFADVAR GSLQSSSFRG
     NPVTLTTVDL QEVLAEAF
//
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