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Database: UniProt
Entry: A8FGM3_BACP2
LinkDB: A8FGM3_BACP2
Original site: A8FGM3_BACP2 
ID   A8FGM3_BACP2            Unreviewed;       402 AA.
AC   A8FGM3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:ABV63390.1};
GN   OrderedLocusNames=BPUM_2734 {ECO:0000313|EMBL:ABV63390.1};
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV63390.1, ECO:0000313|Proteomes:UP000001355};
RN   [1] {ECO:0000313|EMBL:ABV63390.1, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV63390.1,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007358}.
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DR   EMBL; CP000813; ABV63390.1; -; Genomic_DNA.
DR   RefSeq; WP_012011016.1; NZ_VEIS01000024.1.
DR   AlphaFoldDB; A8FGM3; -.
DR   STRING; 315750.BPUM_2734; -.
DR   KEGG; bpu:BPUM_2734; -.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_0_0_9; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000001355; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08551; Fe-ADH; 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.
DR   PROSITE; PS00060; ADH_IRON_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          19..385
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   402 AA;  43439 MW;  35B33C7BCDC9D912 CRC64;
     MTLNMKIESM QKFHTFEIPT VIKHGIGSVK HVGEEVKAYG VSKVLLVTDP GIYLAGVVNP
     VIASLKEAQI DVVLFDKVEP NPPVRLVNEG SALYEKEGCN GLVAVGGGSS MDTAKAIGVE
     ATHEGSVLDY EAAEGKKPLE NRIPPLTTIP TTAGTGSEVT QWAVITDEER EFKFNTGGPL
     IAAHLTVIDP ELHVSMPPHV TAMTGIDALA HAIECYTMKF AQPITDAVAL MAIEYAAHYI
     RRAFADGEDI EARYGMAQAA MLAGLSYGSE SAGAAHAMSQ TLGGMIPVAH GQCVAAMMGP
     VMEYNWKGYP EKFARIAQAF GIDTSRMSTE EAAKAAVNWM YDLVEDLEVP SLEEQGVSKE
     MIDRLSKEAM KDPQTIGNPR DLNEKAYNWI YARCFDLTPK TV
//
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