ID   A6FGT4_9GAMM            Unreviewed;       881 AA.
AC   A6FGT4;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=PE36_02809 {ECO:0000313|EMBL:EDM65667.1};
OS   Moritella sp. PE36.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=58051 {ECO:0000313|EMBL:EDM65667.1, ECO:0000313|Proteomes:UP000004278};
RN   [1] {ECO:0000313|EMBL:EDM65667.1, ECO:0000313|Proteomes:UP000004278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PE36 {ECO:0000313|EMBL:EDM65667.1,
RC   ECO:0000313|Proteomes:UP000004278};
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 (JUN-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:EDM65667.1}.
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DR   EMBL; ABCQ01000045; EDM65667.1; -; Genomic_DNA.
DR   RefSeq; WP_006033591.1; NZ_ABCQ01000045.1.
DR   AlphaFoldDB; A6FGT4; -.
DR   STRING; 58051.PE36_02809; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000004278; 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          7..269
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   881 AA;  95617 MW;  E1BF4DD16527A4A3 CRC64;
     MTVKNIETLN AMVAKVKTAQ QEFATFNQQQ VDKIFRAAAL AASTARIPLA QMAVEESGMG
     VLEDKVTKNH FASEYIYNKY KDSLTCGIIE EDTEFGTITI AEPVGIICGI VPTTNPTSTA
     IFKALISLKT RNGIIFSPHP RAKNATNTAA KIVLDAAVAA GAPQHIIGWI DEPSVELSNS
     LMHHNDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPIV IDETADIKRA VSSILMSKTF
     DNGVVCASEQ AVIVVDEVYD AVKARFITHG GYILTKKEAD KVREIVLING NMNPAIVGQS
     AIKIAKMAGV TVPPFTKVLI GEGPEVHVDD AFAHEKLSPT LGMFRARDYN HAVEQAITMV
     ELGGIGHTSG LYTDQDANEE RIKDFGDKMK TARILINQPS SQGGIGDLYN FGLAPSLTLG
     CGSWGGNSIS ENVGPKHLIN KKIVAKRAEN MLWHKLPESI YFRRGSLPIA MDDLVGKKRA
     CIVTDKFLFN NGYVDDLVSI LKSKGIDTEV FYDVEADPTL AIVKKGVAVM NSFQPDVIIA
     FGGGSPMDAA KIMWVMYEHP DVHFEDLAMR FMDIRKRIYK FPKMGIKAMM VAVTTTSGTG
     SEVTPFAVVT DEVTGQKYPI ADYQLTPNMA VIDANLVMNM PKSLTAFGGY DAVTHALEAY
     VSVLQNEYSD GQALQALKLL KEYLPSSYKN GAKDPIAREK VHNGATIAGI AFANAFLGVC
     HSMAHKIGAE FHIPHGLANA LLITNVIRYN ATDMPTKQAA FSQYDRPKAR ARYAEVAEHL
     GFREGKTADK VHALLNWLDE LKTELDIPKS IQAAGVNEAD FLAKVDQLAI EAFDDQCTGA
     NPRYPLISEL KALLLASYYG NDYQESYVLE KQAAIKETVK K
//