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Database: UniProt
Entry: R2XFR0_9ENTE
LinkDB: R2XFR0_9ENTE
Original site: R2XFR0_9ENTE 
ID   R2XFR0_9ENTE            Unreviewed;       866 AA.
AC   R2XFR0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=UKC_03636 {ECO:0000313|EMBL:EOI53684.1};
OS   Enterococcus gilvus ATCC BAA-350.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1158614 {ECO:0000313|EMBL:EOI53684.1, ECO:0000313|Proteomes:UP000013750};
RN   [1] {ECO:0000313|EMBL:EOI53684.1, ECO:0000313|Proteomes:UP000013750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-350 {ECO:0000313|EMBL:EOI53684.1,
RC   ECO:0000313|Proteomes:UP000013750};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterococcus gilvus ATCC BAA-350.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the iron-containing
CC       alcohol dehydrogenase family. {ECO:0000256|ARBA:ARBA00035645,
CC       ECO:0000256|PIRNR:PIRNR000111}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00035641,
CC       ECO:0000256|PIRNR:PIRNR000111}.
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:EOI53684.1}.
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DR   EMBL; AJDQ01000012; EOI53684.1; -; Genomic_DNA.
DR   RefSeq; WP_010781976.1; NZ_KB946874.1.
DR   AlphaFoldDB; R2XFR0; -.
DR   PATRIC; fig|1158614.3.peg.3622; -.
DR   eggNOG; COG1012; Bacteria.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_1_0_9; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000013750; Unassembled WGS sequence.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR   GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR   CDD; cd08178; AAD_C; 1.
DR   CDD; cd07122; ALDH_F20_ACDH; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR034789; AAD_C.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012079; Bifunc_Ald-ADH.
DR   PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR11496:SF83; HYDROXYACID-OXOACID TRANSHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PIRSF; PIRSF000111; ALDH_ADH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000111}.
FT   DOMAIN          17..406
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          464..850
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   866 AA;  94151 MW;  D93888D618BAAE11 CRC64;
     MAKAIEKEKD AVSVEQVIDE LATKANVALK EMEDFDQEKI DHIVHEMAMA ALDKHMLLAK
     MAVEETGRGV VEDKAIKNMY ASEYIWNSIK HDKTVGVIGE DKQKGLIEVA GPVGVVCGVT
     PTTNPTSTTI FKSMIALKTG NPIVFAFHPS AQKCSAEAAR IVRDAAIAAG APENCIQWIE
     KPSIDATSML MNHPGVAIVL ATGGPGMVKS AYSTGKPALG VGAGNVPSYI EKTAKIKRAV
     NDLIVSKSFD NGMICASEQA VIVDKEVYEE VKAEFQAHQV YVVKKAELKR LEDAVMNEGK
     YAVNPAIVGH SAEDIAQRAG IKVPAGTKIL IAELDGVGAD YPLSREKLSP VLAMIKANDH
     VHGFDLCQGM LELGGLGHTA VIHTEDEDLQ VKFGLRMKAC RILVNSPSAE GGIGDIYNEM
     IPSLTLGCGS YGKNSVSKNV SAINLINVKT IAKRRNNMQW FKLPPKIFFE KNSLLYLTKM
     ENVERVMLVC DPGMVQFGYA DIVREVLGRR ENDVKVEVFS DVEPNPSTNT VYKGLEMFND
     FQPDTVIALG GGSAMDAAKG MWMFFEHPDT SFFGAKQKFL DIRKRTYGIA KPEKAKLVCI
     PTTSGTGAEV TPFAVITDSE THVKYPLADY ALTPDVAIVD PQFVMTVPAS VTADTGMDVL
     THAIESYVSV MASDYTRGLS LQAIKLVFEN LEKSVKTADP EAREKMHNAS AMAGMAFANA
     FLGICHSVAH KIGGEYGIPH GRTNAILLPH IIRYNAKDPQ KHAMFPKYDY FRADTDYADI
     AKFLGLKGNT TAELVEALIE AVYNLGVTTG IDMNLKAQGV TQETLNTTVD RMAELAYEDQ
     CTTANPKEPL ISELKEIIVT AYDYKA
//
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