ID   A4Y6F2_SHEPC            Unreviewed;       870 AA.
AC   A4Y6F2;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   OrderedLocusNames=Sputcn32_1811 {ECO:0000313|EMBL:ABP75535.1};
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP75535.1};
RN   [1] {ECO:0000313|EMBL:ABP75535.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 {ECO:0000313|EMBL:ABP75535.1};
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-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; CP000681; ABP75535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4Y6F2; -.
DR   STRING; 319224.Sputcn32_1811; -.
DR   KEGG; spc:Sputcn32_1811; -.
DR   eggNOG; COG1012; Bacteria.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_2_1_6; -.
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          5..268
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          457..845
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   870 AA;  93797 MW;  9237FBBF2C1FF8B8 CRC64;
     MLVTNAQELD LMVERVAKAQ AEYATFSQEQ VDAIFRAAAL AAADARISLA KMAAAETRMG
     VIEDKVIKNH FASEYIYNKY KDEKTCGILS EDLTFGTITI AEPVGIICGI VPTTNPTSTA
     IFKALISLKT RNAIIFSPHP RAKASTTTAA KLVLDAAVAA GAPKDIIGWI DEPSVALSNQ
     LMTHPKVNLI LATGGPGMVK AAYSSGKPAI GVGAGNTPIV IDETADIKRA VSSILMSKTF
     DNGVVCASEQ AVIVVDSIYE QVKERFASHG GYILSASETA AMQNVILKNG GLNADIVGQS
     AASIAKMAGV EVPHWTKVLI GEVTDISESE AFAHEKLSPL LGMYRAKDFN DAVDQAEALV
     ALGGIGHTSG LYTDQDTQTE RVKTFGFRMK TARILINTPA SQGGIGDLYN FKLAPSLTLG
     CGSWGGNSIS ENVGPSHLIN KKTVAKRAEN MLWHKLPSSI YFRRGSLPIA LEELSDKKRA
     LIVTDRFLFN QGYCNETIRI LKAQGLETEI FYDVEADPTL AIVRQGAKVA CSFKPDVIIA
     LGGGSPMDAA KIIWVMYEHP EVDFADLALR FMDIRKRIYK FPKMGTKAMM VAIPTTSGTG
     SEVTPFAVVT DEQTGKKYPI ADYQLTPNMA IVDPNLVMDM PKSLTAFGGI DAVTHALEAY
     VSVMANEYSD GQALQALDLL CKYLPDAYNL GAQSPVAREK VHNGATIAGI AFANAFLGIC
     HSMAHKLGAE FHLAHGLANA LLINNVIRFN ATDLPTKQAA FSQYDRPKAL CRYAAIADHL
     KLGGKSDEEK VEKLLEKITQ LKKTIGIPAS IQEAGVNEAD FLAKLDVLAE DAFDDQCTGA
     NPRYPLINEL KQLLLDSYYG RDYSDNYTTK
//