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Database: UniProt
Entry: A0A0R1MK31_9LACO
LinkDB: A0A0R1MK31_9LACO
Original site: A0A0R1MK31_9LACO 
ID   A0A0R1MK31_9LACO        Unreviewed;       382 AA.
AC   A0A0R1MK31;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Lactaldehyde reductase {ECO:0000313|EMBL:KRL05717.1};
GN   ORFNames=FD46_GL000468 {ECO:0000313|EMBL:KRL05717.1};
OS   Liquorilactobacillus oeni DSM 19972.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423777 {ECO:0000313|EMBL:KRL05717.1, ECO:0000313|Proteomes:UP000051686};
RN   [1] {ECO:0000313|EMBL:KRL05717.1, ECO:0000313|Proteomes:UP000051686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19972 {ECO:0000313|EMBL:KRL05717.1,
RC   ECO:0000313|Proteomes:UP000051686};
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   -!- 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:KRL05717.1}.
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DR   EMBL; AZEH01000020; KRL05717.1; -; Genomic_DNA.
DR   RefSeq; WP_057895459.1; NZ_AZEH01000020.1.
DR   AlphaFoldDB; A0A0R1MK31; -.
DR   STRING; 1423777.FD46_GL000468; -.
DR   PATRIC; fig|1423777.3.peg.489; -.
DR   Proteomes; UP000051686; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR11496:SF83; HYDROXYACID-OXOACID TRANSHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051686}.
FT   DOMAIN          64..374
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   382 AA;  41908 MW;  07FADC6B31B4B561 CRC64;
     MDSKIKGMFY LSSFVVRPLI QTSDNLQEFF KAIHVSNKDV LLTNRYIIEP HLKLADLPVD
     AIFVEDYLHG EPTDVAADKL LLKLNEKHYK RVIAIGGGSV IDNAKLSVYG EGLTISDLVK
     NGKTLPQKRK LIIVPTTTGT GSEVTNVAVF NFVSKKTKIG LAYDQMYADQ VFLIGQLATT
     MPYKVFATSS IDALVHSIES YISPKATSFS KSFSLSAMKA ILRGYTKMII TNATGKTPHG
     QELQSFLEAS TQAGIAFGNA GCGAVHALAY PIGSEFHIAH GQSNYLVFSG TFKKYQELGA
     DLSNLEVVLA GELSVQPNEV WTRLENIINS ILPNQHLSEI GMDKKLCQEF AKSVLENQQR
     LLVNAPVKLT EADVADIYTK LL
//
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