ID A0A087EBV7_9BIFI Unreviewed; 912 AA.
AC A0A087EBV7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN ORFNames=BISU_1378 {ECO:0000313|EMBL:KFJ05258.1};
OS Bifidobacterium subtile.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=77635 {ECO:0000313|EMBL:KFJ05258.1, ECO:0000313|Proteomes:UP000029055};
RN [1] {ECO:0000313|EMBL:KFJ05258.1, ECO:0000313|Proteomes:UP000029055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11597 {ECO:0000313|EMBL:KFJ05258.1,
RC ECO:0000313|Proteomes:UP000029055};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFJ05258.1}.
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DR EMBL; JGZR01000001; KFJ05258.1; -; Genomic_DNA.
DR RefSeq; WP_024464328.1; NZ_JGZR01000001.1.
DR AlphaFoldDB; A0A087EBV7; -.
DR STRING; 77635.BISU_1378; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR OrthoDB; 323926at2; -.
DR Proteomes; UP000029055; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029055}.
FT DOMAIN 19..286
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 476..874
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 99279 MW; E4E49C3DA5A44EAE CRC64;
MADAKKNSTA GKPSAEDKQA AAQSEVDALV KRGLKALEEF EELDQEQVDR IVGKASIAAL
KNHLVLAKMA VDETGRGLVE DKATKNIFAC EHVTHYLSGQ KTVGIINEDD VLGIDEVAEP
VGVVAGVTPV TNPTSTAIFK SLIALKTRCP IVFGFHPFAQ KCSVEAARIV RDAAVAAGAP
KDCIQWIEHP SIAATGALMQ HPGIATILAT GGPGMVKAAY TSGKPALGVG PGNAPAYVDN
DVDVVRAAND LVLSKHFDYG MICATEQAII AHADIYDPLV AELKRRKAYF VNEEEKAKLE
QYMFGCTSYS GGTPSLNSVV PGKSPQFIAQ AAGFEVPQDA TILVAECREV GEMEPLTMEK
LCPVHALLKA KDKDQAFTMC EQMLVHGAGH SAAIHTNNQD LVREYGLRMH ACRIIWNQPS
SLGGIGDIYN SIAPSLTLGC GSYGGNSVSG NVQAVNLINV KRIARRNNNM QWFKVPAKTY
FEPNAIRYLR DMYNIRRAVI ICDKVMEQLG VVDKVIDQLR ARPELVTFRI IDYVEPEPSV
ETVERGAAMM REEFEPDTII AVGGGSPMDA AKIMWLLYEH PEISFDDVRE KFFDIRKRAF
RIPPLGKKAR LVCIPTSSGT GSEVTPFAVI TDHKTGYKYP ITDYALTPTV AIVDPVLART
QPHTLAQDAG FDSLTHAMES FVSVYANDFT DAMALHAAKL IWDNLADSVN AAPGLRRTEA
QEKMHNAATM AGMAFGSAFL GMCHGMAHTI GALCGIAHGH TNGVLLPYVI RYNGSIPQEA
TSWPKYNKYV APQRYREFAK VLGVDPGATD AEGVENLARA VEDYRDNKLD MDKSFQACGV
DEDYFWSILD QIGMRAYEDQ CTPANPRVPM IEDMKDIAIA AYYGVSQAEG HRLRAERESK
SATIEASQVA KD
//
