ID   F3MHH0_9BACL            Unreviewed;       870 AA.
AC   F3MHH0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   Name=adh {ECO:0000313|EMBL:EGG32457.1};
GN   ORFNames=HMPREF9412_5501 {ECO:0000313|EMBL:EGG32457.1};
OS   Paenibacillus sp. HGF5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=908341 {ECO:0000313|EMBL:EGG32457.1, ECO:0000313|Proteomes:UP000004272};
RN   [1] {ECO:0000313|EMBL:EGG32457.1, ECO:0000313|Proteomes:UP000004272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGF5 {ECO:0000313|EMBL:EGG32457.1,
RC   ECO:0000313|Proteomes:UP000004272};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (FEB-2011) 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:EGG32457.1}.
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DR   EMBL; AEXS01000163; EGG32457.1; -; Genomic_DNA.
DR   RefSeq; WP_009595009.1; NZ_AEXS01000163.1.
DR   AlphaFoldDB; F3MHH0; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000004272; 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}.
FT   DOMAIN          14..410
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          466..852
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   870 AA;  95670 MW;  5EEABDDD4026311A CRC64;
     MAVSKGTTVE VKGQTAAEYI QGLIDKANRA KEKFMKLDQE QVDGIVQAMA MAGLEKHMQL
     AKMAVEETGR GVYEDKIIKN LFATEYIHNS IKYDKTVGII EDNAYDSFQK IAEPIGIIMG
     ITPVTNPTST TIFKALISIK TRNPIIFGFH PSAQACSREA ALILRDAAVK QGAPADCIQW
     IEAPSMDKTN TLMNHPDVAC ILATGGSAMV KAAYSCGKPA LGVGPGNVPC FIEKSADLDQ
     AVNDLILSKT FDNGMICASE QAVIIEEPIY HTVKKKMIAS GCYFVNKEEQ AKLTAHAMVA
     DKCAVNPTIV GQPAAKIAEA CGFEVPESTK ILVAELEGVG PAYPLSAEKL SPVLACYKVK
     DAEEGITRAE EMVAFGGMGH SSVIHSHNED VILKFSDRMK TCRILVNQPS SQGGIGDIYN
     TNLPSLTLGC GSYGRNSTSS NVTAVNLINV KRVNRRTVNM QWFKVPDKIY FEKGSTQYLA
     KMPDITRVAI VTDPMMVKLG YVERVEHYLR QRRLPVAIEV FSEVEPDPST TTVERGTEML
     ERFQPDCIIA LGGGSPMDAA KAMWLFYEYP DTDFNNLKQK FMDIRKRVYK YPKLGRKAKF
     VAIPTTSGTG SEVTSFAVIT DKVQGNTKYP LADYELTPDV AIIDPEFVYT LPKTAVADTG
     MDVLTHAIEA YVSVMASDYT DGLAIKAIQL VFQYLEQSAL TGNKLAREKM HNASTLAGMA
     FANAFLGINH SLAHKWGGQY HTAHGRTNAI LMPHVIRYNA KKPTKFAAWP KYTHFVADER
     YAEIARILGL PARTTEEGVN SLIAAIRELN SKLGIEESFQ QLGIDPQDFE RNVEHLADRA
     FEDQCTTSNP KLPLVTELAE VYRNAFYGRF
//