ID A4J4M2_DESRM Unreviewed; 863 AA.
AC A4J4M2;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN OrderedLocusNames=Dred_1495 {ECO:0000313|EMBL:ABO50025.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50025.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO50025.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50025.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) 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}.
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DR EMBL; CP000612; ABO50025.1; -; Genomic_DNA.
DR RefSeq; WP_011877841.1; NC_009253.1.
DR AlphaFoldDB; A4J4M2; -.
DR STRING; 349161.Dred_1495; -.
DR KEGG; drm:Dred_1495; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_1_0_9; -.
DR OrthoDB; 9804734at2; -.
DR Proteomes; UP000001556; Chromosome.
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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001556}.
FT DOMAIN 14..266
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 460..850
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 863 AA; 94722 MW; F092F61040A4A8EB CRC64;
MSEQKPDQNI SVTINGLVKK ARQAQEEYLH LNQEQVDNIV KAMALAGLEN HMGLAKMAVI
DTKRGVYEDK ITKNIFATEE VYHSIKYERT VGIINENTEE NFLEVAEPIG VVAAVVPVTN
PTSTTMFKAL ICAKTRNPVV FSFHPGALKC SIAAAKVMLE AAIAAGAPKD CISWIEKPSV
EATQQLMAHP GVSLILATGG TNMVCSAYSS GKPALGVGPG NVPCYIEKTA NIRRAVTDLI
LSKTFDNGMI CASEQAVIID REIADLTIGY LRDSGCYILS PTEIEQLNKA AIDHDAGFID
PQIVGQPATH IAEMAGISVP SGTKILVAPL EGVGPEYPLS MEKLSPILAL YIVNSSEEGI
QRCVDMLEFG GLGHSAVLHS ENEELIKHFS QVVRAGRIIV NSPSTHGAIG DIYNTNVPSL
TLGCGSMGRN STTANVSVKN LINVKRVATR KEKMQWFRVP ERIYFMPGSI QYLTKMPDVQ
KVLIVTDKVM NDMGYVERVT YHLRKRQNDV QIEVFDLVEP DPPIEIVSQG VELMEKFNPD
TLIALGGGSS IDTAKGMWLL YEYPEMKFEF LKLKFLDIRK RTYKYPKLGR KVKLVAVPTT
SGSGSEITAF TVISDKQRKV KYPLADYELT PDVAIIDSDF VMSVPPKVTA DTGIDVLTHA
IEAYVAVMAS DYTDGLALKA IELVFAYLPR VYKNGQDKEA RIKMHNASAI AGMAFTNAFL
GINHSMAHIL GAKFGLSHGR ANGVLLPYVI EYNASYPSKF AAFPNYEYYV APEKYQQIAR
YLGLPSQTVE EGVHSLVGAI RNLMQQLDIP LTIADCGIPK AEFEAAVPEM SERAFEDQCT
TSNPRMPLIE ELKEIYRRAY GNA
//
