ID F3Y9I2_MELPT Unreviewed; 863 AA.
AC F3Y9I2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN OrderedLocusNames=MPTP_0693 {ECO:0000313|EMBL:BAK21160.1};
OS Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB
OS 702443).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Melissococcus.
OX NCBI_TaxID=940190 {ECO:0000313|EMBL:BAK21160.1, ECO:0000313|Proteomes:UP000008456};
RN [1] {ECO:0000313|EMBL:BAK21160.1, ECO:0000313|Proteomes:UP000008456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443
RC {ECO:0000313|Proteomes:UP000008456};
RX PubMed=21622755; DOI=10.1128/JB.05151-11;
RA Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M.,
RA Miyoshi-Akiyama T.;
RT "Complete genome sequence of Melissococcus plutonius ATCC 35311.";
RL J. Bacteriol. 193:4029-4030(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 35311;
RA Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D.,
RA Akiyama T.;
RT "Whole genome sequence of Melissococcus plutonius ATCC 35311.";
RL Submitted (APR-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}.
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DR EMBL; AP012200; BAK21160.1; -; Genomic_DNA.
DR RefSeq; WP_013773598.1; NC_015516.1.
DR AlphaFoldDB; F3Y9I2; -.
DR STRING; 940190.MPTP_0693; -.
DR KEGG; mps:MPTP_0693; -.
DR HOGENOM; CLU_007207_1_0_9; -.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000008456; 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; 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 Coiled coil {ECO:0000256|SAM:Coils}; 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:UP000008456}.
FT DOMAIN 18..408
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 465..849
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT COILED 680..707
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 863 AA; 93961 MW; 5D7A3658B1E96F3E CRC64;
MAQAKKEVGQ EMDIQTMINE LAGKANVALK EMANFDQEKV DHIVHQMAIA ALDQHMQLAK
LAVEETGRGI VEDKAIKNIY ASEYIWNSIK NNKTVGIINE DDQTGLIEIA EPVGVICGVT
PTTNPTSTTI FKSLIALKTR NPIIFAFHPS AQQCSKKAAM IVRDSAIQAG APENCVQWIE
YPSIEATSAL MNHSGIATVL ATGGAGMVKS AYSTGKPALG VGPGNVPSYI EKTANIKRAV
NDLIISKSFD NGMICASEQA IIVDKEIYAA IKEEFEAHQV YFIKPNELSK LEDAVMNEEK
TAVNPVIVGN SAEVIANLAG IKVPKGTKIL VAELEGVGAK YPLSREKLSP ILAMIKANNT
EQALDLCEAM LELGGLGHTA VIHTEDEGLQ VNFGLRMKAC RILVNSPSAE GGIGNIYNEM
IPSLTLGCGS YGKNSVSKNV SSINLINVKT IAKRRNNMQW IKLPRVYFEK NSLQYLQTME
NVERVMLVCD PGMVQFGYAD IVVKELQKRA NDIKLVTFSE VEPNPSTNTV YAGTKMMREF
EPDTIIALGG GSAMDAAKGM WMFYEHPDTS FFGAKQEFLD IRKRTYKIKK AVKSKLVCIP
TTSGTGAEVT PFAVITDSDT HVKYPLADYA LTPDVAIVDP QFVLSVPASV TADTGMDVLT
HAIESYVSVM ASDYTRGLSL QAIKLVIENL EKSVNTADME AREKMHNAST MAGMAFANAF
LGITHSIAHK IGGEYNIPHG RTVGILLPHV IRYNATDPSK HAMFPKYDYF RADTDYADIA
KFIGLKGKDT AELVEALATT VYELGQKVGI KMNLKDQGVT KAVLDSTVDR MAELSYEDQC
TTANPKEPLI SELKQIIINA YNG
//
