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Database: UniProt
Entry: A0A059KI31_9BURK
LinkDB: A0A059KI31_9BURK
Original site: A0A059KI31_9BURK 
ID   A0A059KI31_9BURK        Unreviewed;       396 AA.
AC   A0A059KI31;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Alcohol dehydrogenase iron-type/glycerol dehydrogenase GldA domain-containing protein {ECO:0000259|Pfam:PF00465};
GN   ORFNames=X805_33180 {ECO:0000313|EMBL:KDB51091.1};
OS   Sphaerotilus natans subsp. natans DSM 6575.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Sphaerotilus.
OX   NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB51091.1, ECO:0000313|Proteomes:UP000026714};
RN   [1] {ECO:0000313|EMBL:KDB51091.1, ECO:0000313|Proteomes:UP000026714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB51091.1,
RC   ECO:0000313|Proteomes:UP000026714};
RX   PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA   Park S., Kim D.H., Lee J.H., Hur H.G.;
RT   "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT   formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL   FEMS Microbiol. Ecol. 90:68-77(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:KDB51091.1}.
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DR   EMBL; AZRA01000100; KDB51091.1; -; Genomic_DNA.
DR   RefSeq; WP_037484328.1; NZ_AZRA01000100.1.
DR   AlphaFoldDB; A0A059KI31; -.
DR   STRING; 34103.SAMN05421778_12832; -.
DR   PATRIC; fig|1286631.3.peg.3239; -.
DR   eggNOG; COG1454; Bacteria.
DR   Proteomes; UP000026714; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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}.
FT   DOMAIN          18..387
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   396 AA;  41147 MW;  F0EFF1F1003123B8 CRC64;
     MFAEPLPAFV FQTVRRIESA PGLARRLGEL VSSLDPPGRS ALIVTDAFLA SSGLIAPARA
     SLEAAGWQVA VFDAVTPDPS EAVVEAARQA ALVHGAGLVI GFGGGSSMDV AKLVACLARP
     EAPALSELYG IDTRVVARLP LVQVPTTAGT GSEVTRIAIV TTGADTKAGV VNRALLADLV
     LLDAELTVGL PPAVSAATGI DAMVHAIEAF TSRLRANPLS DLLAVDALRR LDRHLLATLA
     DGHDLAAREQ MLLGAMLAGM AFENAPVAAV HALAYPLGGQ FHLPHGLSNA LVLTPVLRFN
     RPAAQARYAA LAAQLLPKAS AGLDEAQRCE AFIAHVAQRV ADCAACGLAQ RLRDCGIPRD
     ALPGLAAAAM QQQRLLQNNP RPLTEADALA IYEEAW
//
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