ID   A9DHK4_9GAMM            Unreviewed;       866 AA.
AC   A9DHK4;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=KT99_12369 {ECO:0000313|EMBL:EDP99180.1};
OS   Shewanella benthica KT99.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=314608 {ECO:0000313|EMBL:EDP99180.1, ECO:0000313|Proteomes:UP000005839};
RN   [1] {ECO:0000313|EMBL:EDP99180.1, ECO:0000313|Proteomes:UP000005839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT99 {ECO:0000313|EMBL:EDP99180.1,
RC   ECO:0000313|Proteomes:UP000005839};
RA   Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (OCT-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP99180.1}.
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DR   EMBL; ABIC01000049; EDP99180.1; -; Genomic_DNA.
DR   RefSeq; WP_005502437.1; NZ_ABIC01000049.1.
DR   AlphaFoldDB; A9DHK4; -.
DR   STRING; 314608.KT99_12369; -.
DR   Proteomes; UP000005839; Unassembled WGS sequence.
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   866 AA;  93436 MW;  C2FAD471EBD31E69 CRC64;
     MTVTNEQELD LLVQRVADAQ AQFANFSQER VDIIFRAAAL AAADARISLA KMAVAETRMG
     VVEDKVIKNH FASEYIYNKY KDSKTCGIID EDPTFGTITI AEPVGVICGI VPTTNPTSTA
     IFKALISLKT RNGIIFSPHP RAKKSTTTAA RIVLDAAVKA GAPKDIIGWI DEPSVALSNR
     LMTHDKINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPIV IDETADIKRA VSSILMSKTF
     DNGVVCASEQ AVIVVDEIYD TVKKRFATHG GYILNADESE AMQGVILKNG ALNADIVGQS
     AVDIASMAGI NVPRWTKVLI GEATDISDAE AFAHEKLSPL LGMYRAKDFD DAMDKAEALV
     TFGGIGHTSG LYTNQDTQED RVKAFGFRMK TARILINTPA SHGGIGDLYN FKLAPSLTLG
     CGSWGGNSIS ENVGPSHLIN KKIVAKRAEN MLWHKLPSSI YFRRGCLPIA LEELSDKKRA
     LIVTDKHLFN NGYCDETVNI LKAQGLTTEI FYEVEADPTL AIVKQGAKMA HSFQPDVIIA
     LGGGSPMDAA KIIWVMYEHP DVDFADLALR FMDIRKRIYK FPKLGVKAQM VAIPTTSGTG
     SEVTPFAVVT DEATGMKYPI ADYQLTPNMA IIDPNLVMDM PKSLTAFGGI DAITHALEAY
     VSVMANEYSD GQALQALDLL FKHLPDAYNH GAAAPVAREK VHNGSTIAGI AFANAFLGVC
     HSMAHKLGAE FHLAHGLANA LLISNVIRYN ATDMPTKQAA FSQYDRPKAL CRYAKIADHL
     NLTGNTDEQK VEALLEKIDE LKKTIGIPAS IQEAGVNEAD FLAKLDELAE NAFDDQCTGA
     NPRYPLIAEL KQILLDSFYG NAYSDS
//