ID   A0A3S1DE11_9BACL        Unreviewed;       870 AA.
AC   A0A3S1DE11;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=EJP77_04240 {ECO:0000313|EMBL:RUT36207.1};
OS   Paenibacillus zeisoli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2496267 {ECO:0000313|EMBL:RUT36207.1, ECO:0000313|Proteomes:UP000272464};
RN   [1] {ECO:0000313|EMBL:RUT36207.1, ECO:0000313|Proteomes:UP000272464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-5-3 {ECO:0000313|EMBL:RUT36207.1,
RC   ECO:0000313|Proteomes:UP000272464};
RA   Sun L., Chen Z.;
RL   Submitted (DEC-2018) 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:RUT36207.1}.
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DR   EMBL; RZNX01000001; RUT36207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S1DE11; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000272464; 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:UP000272464}.
FT   DOMAIN          11..409
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          465..852
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   870 AA;  95604 MW;  EEBD54C6BEFB86F5 CRC64;
     MAVKTEVNEP VKPTAEEHIQ TLINKAKKAT DAFMKMDQEQ IDKIVQAMAL AGMDKHMYLA
     KLAIEETGRG VYEDKIIKNM FATEYIYHSI KNNKTVGVIE DNPFDNFQKI AEPVGIIMGI
     TPVTNPTSTT IFKALIAIKT RNPIIFGFHP SAQGCCTETA QILLKAAVEN GAPADCIQWI
     EAPSMDKTNA LMNHPDVALI LATGGSAMVR AAYSCGKPAL GVGPGNVPCF IEKSADIDQA
     VNDLILSKTF DNGMICASEQ AVIIEEPIFD QVKKKMIANG CYFVNKEEAA KLTAGAIIAD
     KCAVNPTIVG QPAVKIAEMC GIQVPEGTKI LVAEIEGVGT KFPLSAEKLS PVLACYKVNS
     AQQGIDRAAE VVAFGGMGHS SVIHSNNEEV IQKFSDRMPT CRILVNQPSS QGGIGDIYNT
     NLPSLTLGCG SYGRNSTSSN VTAVNLINVK RVNRRTVNMQ WFKVPSKVYF EKGATQYLAK
     MPDITRVLIV TDPMMVKLGY VDRVEHYLRQ RETPVAIEVF SQVEPDPSTT TVQRGTELMN
     QFQPDCIIAL GGGSPMDAAK GMWLFYEYPD TDFNNLKQKF MDIRKRIYKY PRLGQKAQFV
     AIPTTSGTGS EVTSFAVITD KENGNTKYPL ADYELTPDVA IIDPEFVYSL PKVAVADTGM
     DVLTHAIEAY VSVMASDYTD GLAIKAIQLV FEWLEKSALT GDKLAREKMH NASTLAGMAF
     ANAFLGINHS LAHKWGGQYH TAHGRTNAIL MPHVIRYNAK KPTKFAAFPK YTNFVADQRY
     AEIARILGLP ARTTEEGVKS LINAIRDMNK KLGIPESFQE LGFDPKDFES RVDYLADRAF
     EDQCTTANPK LPLVKELAEV YRDAFYGRFE
//