ID A1S693_SHEAM Unreviewed; 867 AA.
AC A1S693;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN OrderedLocusNames=Sama_1693 {ECO:0000313|EMBL:ABL99899.1};
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABL99899.1, ECO:0000313|Proteomes:UP000009175};
RN [1] {ECO:0000313|EMBL:ABL99899.1, ECO:0000313|Proteomes:UP000009175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175};
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) 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; CP000507; ABL99899.1; -; Genomic_DNA.
DR RefSeq; WP_011759807.1; NC_008700.1.
DR AlphaFoldDB; A1S693; -.
DR STRING; 326297.Sama_1693; -.
DR KEGG; saz:Sama_1693; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_2_1_6; -.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000009175; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009175}.
FT DOMAIN 5..267
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; 93034 MW; 6745947CBFDB52A0 CRC64;
MTVTNTQELN ELVARVAKAQ AQFASYSQEQ VDRIFRAAAL AAADARIRLA KMAAEETRMG
VVEDKVIKNH FASEYIYNKY KDEKTCGILA EDATFGTITI AEPVGIICGI VPTTNPTSTA
IFKALISLKT RNGIIFSPHP RAKVSTTTAA RIVLDAAIAA GAPKDIIGWI DEPSVALSNQ
LMTHEKINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPIV IDETADIKRA VSSILMSKTF
DNGVVCASEQ AVVVVDAVYD AVKERFSSHG GYLLSKKENA ALQKVILKDG GLNADIVGQS
AATIAAMANI KVPAHTKVLI GEVTDIDEKE AFAHEKLSPL LGMYRAANFE EALDKAEALV
ALGGIGHTSG LYTDQDTQDE RVKSFGYRMK TARILINTPA SQGGIGDLYN FKLAPSLTLG
CGSWGGNSIS ENVGPSHLIN KKTVAKRAEN MLWHKLPSSI YFRRGSLPIA LEELSGKKRA
LIVTDKFLFN NGYCDETIRI LKSQGLETEV FYEVEADPTL AVVRAGAKVA TSFQPDVIVA
LGGGSPMDAA KIIWVMYEHP DVDFADLALR FMDIRKRIYK FPKLGAKAMM VAIPTTSGTG
SEVTPFAVVT DEQTGAKYPI ADYELTPNMA IVDPNLVMDM PKSLTAFGGI DAITHALEAY
VSVMANEYSD GQALQALDLL FKYLPDSYAR GAQAPLAREK VHNGATIAGI AFANAFLGIC
HSMAHKLGAE FHLPHGLANA LLISNVIRFN ATDLPTKQAA FSQYDRPKAL CRYAAIASHL
GLAGNNDEAK VEALIAKIEE LKAAIGIPVS IKDAGVNEAD FMAKLDELAE DAFDDQCTGA
NPRYPLISEL KQLLIDSFHG RAYQDSL
//
