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Database: UniProt
Entry: A3D3W5_SHEB5
LinkDB: A3D3W5_SHEB5
Original site: A3D3W5_SHEB5 
ID   A3D3W5_SHEB5            Unreviewed;       867 AA.
AC   A3D3W5;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   OrderedLocusNames=Sbal_1922 {ECO:0000313|EMBL:ABN61428.1};
OS   Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN61428.1, ECO:0000313|Proteomes:UP000001557};
RN   [1] {ECO:0000313|EMBL:ABN61428.1, ECO:0000313|Proteomes:UP000001557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557};
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.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA   Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS155.";
RL   Submitted (FEB-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; CP000563; ABN61428.1; -; Genomic_DNA.
DR   RefSeq; WP_011846673.1; NC_009052.1.
DR   AlphaFoldDB; A3D3W5; -.
DR   STRING; 325240.Sbal_1922; -.
DR   KEGG; sbl:Sbal_1922; -.
DR   HOGENOM; CLU_007207_2_1_6; -.
DR   OMA; QWFKVPP; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000001557; 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.
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          4..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   867 AA;  93774 MW;  83A4170C12795743 CRC64;
     MTVTNAQELD LMVERVAKAQ AEYATFSQAQ VDKIFRAAAL AAADARISLA KMAAAETRMG
     VVEDKVIKNH FASEYIYNKY KDEKTCGILS EDVTFGTITI AEPVGIICGI VPTTNPTSTA
     IFKALISLKT RNAIIFSPHP RAKVSTTTAA KLVLDAAIAA GAPKDIIGWI DEPSVALSNQ
     LMTHPKVNLI LATGGPGMVK AAYSSGKPAI GVGAGNTPIV IDETADIKRA VSSILMSKTF
     DNGVVCASEQ AVIVVDSIYE QVKERFISHG GYMLSKDETA AMQHVILKNG GLNADIVGQS
     AASIAQMAGF EVPHWTKVLI GEVTDICDSE AFAHEKLSPL LGMYRAIDFN DAMDKAEALV
     ALGGIGHTSG LYTDQDTQTE RVHAFGFRMK TARILINTPA SQGGIGDLYN FKLAPSLTLG
     CGSWGGNSIS ENVGPSHLIN KKTVAKRAEN MLWHKLPASI YFRRGSLPIA LEELSDKKRA
     LIITDRFLFN HGYCDETMRI LKAQGLETEI FYDVEADPTL AIVRQGAKVA QSFKPDVIIA
     LGGGSPMDAA KIIWVMYEHP DVDFADLALR FMDIRKRIYK FPKMGTKAMM VAIPTTSGTG
     SEVTPFAVVT DEITGKKYPI ADYQLTPNMA IVDPNLVMDM PKSLTAFGGI DAVTHALEAY
     VSVMANEYSD GQALQALDLL CKYLPDAYNL GSQSPVAREK VHNGATIAGI AFANAFLGIC
     HSMAHKLGAE FHLAHGLANA LLINNVIRFN ATDLPTKQAA FSQYDRPKAL CRYAAIADHL
     KLGGKTDEEK VEKLLEKITH LKKTIGIPAS IQEAGVNEAD FLAKLDELAE DAFDDQCTGA
     NPRYLLINEL KQLFLDSYYG RDYSDNN
//
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