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Database: UniProt
Entry: A0A0D6A4J4_9LACO
LinkDB: A0A0D6A4J4_9LACO
Original site: A0A0D6A4J4_9LACO 
ID   A0A0D6A4J4_9LACO        Unreviewed;       874 AA.
AC   A0A0D6A4J4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=LBAT_1353 {ECO:0000313|EMBL:BAQ57742.1};
OS   Lactobacillus acetotolerans.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1600 {ECO:0000313|EMBL:BAQ57742.1, ECO:0000313|Proteomes:UP000035709};
RN   [1] {ECO:0000313|EMBL:BAQ57742.1, ECO:0000313|Proteomes:UP000035709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 13120 {ECO:0000313|EMBL:BAQ57742.1,
RC   ECO:0000313|Proteomes:UP000035709};
RA   Toh H., Morita H., Fujita N.;
RT   "Complete genome sequence of Lactobacillus acetotolerans NBRC 13120.";
RL   Submitted (MAR-2015) 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}.
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DR   EMBL; AP014808; BAQ57742.1; -; Genomic_DNA.
DR   RefSeq; WP_060459718.1; NZ_AP014808.1.
DR   AlphaFoldDB; A0A0D6A4J4; -.
DR   STRING; 1600.LBAT_1353; -.
DR   KEGG; lae:LBAT_1353; -.
DR   PATRIC; fig|1600.4.peg.1381; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000035709; Chromosome.
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; 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.
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:UP000035709}.
FT   DOMAIN          22..282
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          469..857
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   874 AA;  96004 MW;  8A8F3C98C3BFD87D CRC64;
     MAKAQQKETV TEEDKNKQIY NMVDDLVKKS HVALDKMANF SQEQVDKICE AIAIAGERSA
     YPLAKMAVEE TGRGVVEDKT TKNMFASENI WNSLRHEKTV GVIKEDKEQG LTKIAEPVGV
     IAGVTPVTNP TSTVVFKSMI ALKTRNTIIF GFHPQAQKCC VKTAEIIREA AIKAGAPENC
     IQWIEKPSME ATNDLMANPG VQTILATGGP GMVKAAYSSG KPALGVGPGN GPSYIEKTAN
     IARAVYDIVL SKTFDNGMVC ASENSVVVDD EIYDQVKEEF KKWNCYFLNP AEIKKFETHF
     IDPRRGTVAG PVAGRSALKI AKLCGVNVPA DTKVIIAEYK GVGKKYPLSA EKLSPVFTLY
     RAKNHEDGFR ICTNLLNYGG RGHTAGIHTS DDDLVRKFAN SMSACRILVN TPAALGGIGD
     LYNNMTPSLT LGTGSYGANS MSHNISAMDL LNIKTVAKRR DNMQWIKVPT KTYFEHNAAN
     YLRHMPNVNR FFIVTDEGVA EQGFADEITD IISKRRGTKE YEVFKAVSLN PTTDIVKDGV
     HRMNIFKPDV IIAIGGGSVM DAAKAMRLFY ENPDMSFEDA YQKFLDIRKR VVRFPTSNDV
     QLVCIPTTSG TGSEVSPVAI IKDTETGIKH TLCDYALIPD VSIVDDQFVE KLPKRLIAWS
     GFEALGHAIE SYVSTMATDF TRGWSIEAIQ TIFNNLKASY DGDLDARKRM HDAATIAGMA
     YSNAFLGLEH SIAHTVGSTF DIPSGVSDAI ALPQVIRFNA KRPKKLAMWP HYSVYRAESD
     YAHIARSLGL TGADDHELVE KLVQKIIDLA HSVGIRLAFK EYGIDKNKFN AKVNSLAVEA
     YGDQNTVTNP LAPLVEQIVQ LMKDCYEGKG INKK
//
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