ID A0A0R2CVY5_9LACO Unreviewed; 896 AA.
AC A0A0R2CVY5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN ORFNames=FC80_GL000218 {ECO:0000313|EMBL:KRM92038.1};
OS Liquorilactobacillus cacaonum DSM 21116.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423729 {ECO:0000313|EMBL:KRM92038.1, ECO:0000313|Proteomes:UP000051131};
RN [1] {ECO:0000313|EMBL:KRM92038.1, ECO:0000313|Proteomes:UP000051131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21116 {ECO:0000313|EMBL:KRM92038.1,
RC ECO:0000313|Proteomes:UP000051131};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM92038.1}.
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DR EMBL; AYZE01000008; KRM92038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2CVY5; -.
DR STRING; 1423729.FC80_GL000218; -.
DR PATRIC; fig|1423729.3.peg.219; -.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000051131; 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:UP000051131}.
FT DOMAIN 26..287
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 475..888
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 896 AA; 98721 MW; 20707B6B5B1D6EE3 CRC64;
MTMTKKMKKT VSPEEKAEHY EQAEVYTKNL VERALIAEEL YSTYSQAEVD RIVAAAALAG
SEAALELAHE AVIETKRGVV EDKDTKNRFA TENIYNLIKN EKTVGVINED KVAGQVRIAA
PLGVLAGIVP TTNPTSTTMF KTLMALKTRN VIIFAFHPQA QKCSAHAAKI LYDAAVAAGA
PKDIVQWIEV PSLDNTTALI RNSKIASILA TGGPGMVNAA LKSGNPSMGV GAGNGAIFVD
HTADLDRAVE DLLLSKRFDN GMICATENSV VVEEAIYTQW LEKMENKGAY VVPKKDYQKV
ADFVFNDNHG VNGPVAGKSA SWIAKEAGIS LPNDKDVMLF ELDAKNIGEK LSSEKLSPLL
SVYKAHTRQE GIKIVTALLD YQGAGHNAAI QIGSQSDPFI TEYAKQTKAA RILVNQPDSI
GGIGDIYTDA LRPSLTLGTG SWGKNSLSHN LSTNDLLNIK TVAKRRNRPQ WVRLPEKIYY
EKNAISYLQD EVEDIKRVFI VADPGMVKFG FVDKIYEQLA LREKMVKSSI YGTVKPDPTL
GQTIEIAKQM GQFKPDTIIA LGGGSALDAA KIARFIYEYS LDQPDGFLDS YEKVSELFTR
LQQKFIDIRK RIVKFHHQLN TQLITIPTTS GTGSEVTPYA VITDDKTHVK YPLTDYELTP
QIAIVDPEFV MTVPQRTVAW SGLDTLSHAL ESYVSVMASD FTRPWSLQAI KLVFENLALS
YKFDSKNPTR AGEKARENMH YAACLAGMAF ANAFLGINHS LAHKTGGEFG LPHGLAISIA
MQHVIRFNGV VGKVKRTPFP RYEVYRGQRD YAEIARFIGL EGNNDAQLVE ALCKKINELM
NEVEVKPTLS ANGVTKENFE KSLGKLIDLV YNDQCTPANP RQPSLEEIKQ LLEDQF
//
