ID A0A1F6RDH3_9BACT Unreviewed; 858 AA.
AC A0A1F6RDH3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN ORFNames=A3B68_01345 {ECO:0000313|EMBL:OGI18669.1};
OS Candidatus Melainabacteria bacterium RIFCSPHIGHO2_02_FULL_34_12.
OC Bacteria; Candidatus Melainabacteria.
OX NCBI_TaxID=1801607 {ECO:0000313|EMBL:OGI18669.1, ECO:0000313|Proteomes:UP000198265};
RN [1] {ECO:0000313|EMBL:OGI18669.1, ECO:0000313|Proteomes:UP000198265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGI18669.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MFRM01000022; OGI18669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6RDH3; -.
DR STRING; 1801607.A3B68_01345; -.
DR Proteomes; UP000198265; 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}.
FT DOMAIN 14..275
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 463..845
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 858 AA; 94043 MW; 438BB93B92E928C2 CRC64;
MDFASELQEN LFPQVDELLL KARKASAVFT QYSQEMVDKI VYTVVRAAIA HSSEFAKLAV
EETRMGLFED KILKNIVASE FLYSQIKDKK TVGIIRELKD EQMVEVAEPV GVIAALTPVT
NPTSTVIYKS IISLKTRNAI VFSPHLMSSK CVAYTAEILY KAALEAGAPE GCIGWLKRNS
KLRKQTNYLL HHKEVDLVFA TGGTTMVRVA YSTGKPAIGV GSGNTPVYVH KSCNVKSTAM
DICISKTFDY GTECPSEQTI VTDKEIYDSL LLEFKRLNCH ICTKNETEKL IPVVIDPDTG
AMNYRYVGKS AFVIAKAAGF SVPSDTKILI CEVNSNDKSN PLLKEKLMPV LAFLAADSES
DALSKCLLVN HSGGTGHTAG IFANNEEVIS NFQNLINAGR IIINQPTSLG GLGGFYNNLP
TTLSFGCGTG GGNSTTENVN IYNLLNIKRS PKRQTSPMWF KIPNQIYFNP GSISVLKTMS
AHNVFIVTSK TMEKSGILKS VIENLPSDIN VKVFSEIEPE PSLDIIHSCL TQIGDFEPDL
FIALGGGSVI DAAKAIRLFY ECPEVKVEDL SVNFLDFRKR VVKFPVLGRT KLVAIPTTSG
TGSEVSPVCV ISDRKDSLKI SLFDYTLAPD IAIIDSELVK DLPLKSTADT AIDAFTHAIE
AFVSIFSSDY TDALCLQAIK LINEYLPKVL QFPNNLEIRQ KLHNAASMAG MAFSNASVGI
NHALAHALGA MYKIPHGRAN AVFLLSTIDF NSGIPRKFMP FSNYKEYIAP EKYAQIAQML
GCTGTDIKEL ISNLKEKVND LLKKSGLPVR VSELGIKLDD YLASIPDLIN KASNDLSLRT
NPRIPIIEEL EVILRNAY
//
