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
//