ID   K6DKU3_9BACI            Unreviewed;       867 AA.
AC   K6DKU3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=BABA_11991 {ECO:0000313|EMBL:EKN68773.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN68773.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN68773.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
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:EKN68773.1}.
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DR   EMBL; AJLS01000063; EKN68773.1; -; Genomic_DNA.
DR   RefSeq; WP_007085414.1; NZ_AJLS01000063.1.
DR   AlphaFoldDB; K6DKU3; -.
DR   STRING; 1117379.BABA_11991; -.
DR   PATRIC; fig|1117379.3.peg.2496; -.
DR   eggNOG; COG1012; Bacteria.
DR   eggNOG; COG1454; Bacteria.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000006316; 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.
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:UP000006316}.
FT   DOMAIN          14..277
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          464..851
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   867 AA;  95232 MW;  6EF693C80739BF2F CRC64;
     MAVKEKVVQE KHLVPEMIDT LANNAAKALG EFRSFNQEMV DEVVKQMALT ALENHRYLAK
     LAVEETKRGV YEDKVFKNMF ATECIYNNIR DMKTVGVISE NENEGMVEMA EPVGVIAGII
     PITNPTSTVI FKSLISLKTR NPIIFAFPRY AQKCCTVTAE LLREAAIKAG APEHCIQWIE
     IPSHEAFQTL MKHPKVSLIL ATGGPNLVTA AYSSGKPALG VGAGNVPCYI EKTANIKRAI
     NDLILSKTFD NGMICASEQA LIIDKEIYDE VRQELIANHC YFLNEEERQL VEQIAIDPKH
     SALNPMIVGL SAYLIAKMAG VNVPVHTKIL IAELEGVGPK YPISCEKLSP LLACYKVNST
     ADGLQIAEET LEYGGLGHSA AIHTADQNLI NQFALRMKAG RIIVNTPSTH GAIGDIYNTS
     LPSLTIGCGT YGGNSVSQNV GAANLINIKK VAKRRKMTQW FKVPSQVFFE QNSIQMLAQI
     PGISKAFIVT SGSSIKNGYV DKVLYYLKKN GAHIQFESFS EVEPDPCIET VMNGAERMKK
     FQPDCIIALG GGSVMDAAKA MWLFYEHPDT DFHSLTQKFF DPSKRVVKFP ALRRKANLVA
     IPTTSGTGSE VTSVTVITDK KTNKKYPLVD FQLTPDIAII DPQFVMTVPK HVTADTGMDV
     LTHAIESYVS VLANDYTDGL ALKAIQLVFE YLPRAFSDGS DELAREKMHN ASTIAGMAFG
     NSFLGINHSL AHVLGAEFSI PHGRANAILL PHVIRYNAAK PNKFMTYPKY EHFIADVRYA
     EIAKMLGLPA STTEEGVDSL IKAIVSLAEK LDIQMSIQAN GVDKEVFENK VALLAEHAFD
     DQDTIANPKQ PFISELAEIY RKAYMGV
//