ID G9ZP24_9LACO Unreviewed; 872 AA.
AC G9ZP24;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN ORFNames=HMPREF9103_01478 {ECO:0000313|EMBL:EHL98435.1};
OS Lentilactobacillus parafarraginis F0439.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=797515 {ECO:0000313|EMBL:EHL98435.1, ECO:0000313|Proteomes:UP000004625};
RN [1] {ECO:0000313|EMBL:EHL98435.1, ECO:0000313|Proteomes:UP000004625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0439 {ECO:0000313|EMBL:EHL98435.1,
RC ECO:0000313|Proteomes:UP000004625};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-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:EHL98435.1}.
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DR EMBL; AGEY01000073; EHL98435.1; -; Genomic_DNA.
DR RefSeq; WP_008212636.1; NZ_JH414968.1.
DR AlphaFoldDB; G9ZP24; -.
DR STRING; 797515.HMPREF9103_01478; -.
DR PATRIC; fig|797515.3.peg.1366; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_1_0_9; -.
DR Proteomes; UP000004625; 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 21..412
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 470..855
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 872 AA; 94769 MW; BC743919B77E422E CRC64;
MIDNKVKAIK TAKPEKTNVD DMINKLVSKA QKALEIMDSF DQEKVDHITH AMVMAGQDKH
MELAIMAAEE TGRGVAEDKA IKNMYATEEI WHSIRDHKTV GVIKNDTERQ LITVAEPLGV
LAGITPVTNP TSTALFKSII AMKTRNPIIF SFHPQAMKSS IAAAKVVRDA AIAAGAPEGA
IQWIDEPSIE ATNKLINNPG VASTLATGGP GMVKAAYSTG KPALGVGPGN GPVYIERTAN
ILRAVNDIVL SKTFDNGMIC ATENSAVIDN EIYDEVKANF VKNGVYFVPK KEQGKLAEAM
FDPQRGSVRG PIAGKSAKAI AKLAGIKVPD NTKVLAAELT GVGKKFPLSA EKLSPVISVY
KAKSHEDAFA ICEALLNFGG LGHTAAIQTT DDDIALKFGV KMKAARVLVN TPGGFGGIGN
LYNEMTPSLT LGTGSWGANS ISHNVTDYDL LNIKTIAKRR NNMQWVKLPR VYFEKTSIRY
LDDMPGINKV FIVTTPGMVE HGYVDKVLDE LKRRPNEIQY SLFSDVEPDP STDTVEKGVA
QMRLFKPDTI IALGGGSPLD AAKNMWLFYE DPKTSFFGAK QKFIDIRKRA YRFNKPRKAQ
MIAIPTTSGT GSEVTPFAVI TDSKTHVKYP LADYALTPDV AIVDPQFVES VPKGTVAASG
LDTLCHGIES FVSTMASDYT RPLSLQAIKL VFDNLTKSYN GDTHAREEMH NAATLAGMAF
GNAFLGITHS VAHKLGGEFG ITHGIAIAIT VPHVIRYNAK LPEKIAVWPK YEYFRANKDY
AEIARYVGVQ GKNDEELIEG LVQKFIDLAH SVGVTLSLKA WGVDKDKFDA AVDRLSVLAY
EDQCTTANPK EPLIADLKQI MIDDYNGTNV EK
//
