ID   A0A1H8KPG3_9FIRM        Unreviewed;       885 AA.
AC   A0A1H8KPG3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=SAMN05216454_1382 {ECO:0000313|EMBL:SEN94785.1};
OS   Peptostreptococcus russellii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptostreptococcus.
OX   NCBI_TaxID=215200 {ECO:0000313|EMBL:SEN94785.1, ECO:0000313|Proteomes:UP000199512};
RN   [1] {ECO:0000313|EMBL:SEN94785.1, ECO:0000313|Proteomes:UP000199512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Calf135 {ECO:0000313|EMBL:SEN94785.1,
RC   ECO:0000313|Proteomes:UP000199512};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FODF01000038; SEN94785.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8KPG3; -.
DR   STRING; 215200.SAMN05216454_1382; -.
DR   OrthoDB; 9804734at2; -.
DR   Proteomes; UP000199512; Unassembled WGS sequence.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1990362; F:butanol dehydrogenase activity; IEA:InterPro.
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; 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; IPR044731; BDH-like.
DR   InterPro; IPR012079; Bifunc_Ald-ADH.
DR   PANTHER; PTHR43633; ALCOHOL DEHYDROGENASE YQHD; 1.
DR   PANTHER; PTHR43633:SF1; ALCOHOL DEHYDROGENASE YQHD; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000111};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199512}.
FT   DOMAIN          28..286
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          477..873
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   885 AA;  97499 MW;  36286304FE49C93F CRC64;
     MTKKLKNEEV EEIKEGQIEE NYIVKDIESF DRRLAQVKKA QEEFAKFSQE EVDKIFLEAA
     LAANHKRLEL AKLAVEETGM GVFEDKVIKN NYAAEYTYNA YKHTKTCGVI EEDKAYGITK
     IAESIGVVAA VIPTTNPTST AIFKTLISLK TRNGIIISPH PRAKKSTIEA AKVVLEAAVK
     AGAPKGIIAW VDEPSIELTA AMMKHADIIL ATGGPGMVKS AYSSGKPALG VGAGNVPALI
     DESADIKTAV SSIILSKSFD NGMICASEQS VIVPDKLYDQ VKKEFEFRGA YILKGEEVDK
     FRKIILNSKG ALNADIVGQS AYQLGKLAGV DVPKSARIVI AEVEETDFVE AFAHEKLSPI
     LAMYKYKSFD EAVAKAEHLV EQGGLGHTSS LYIDTLNCKE KMKKYIDTMK TCRVVINTPS
     AQGGIGDLYN FKLAPSFTLG CGSWGGNSVS ENVGVKHLIN IKTVAERREN MLWFRAPEKV
     YFKKGCLPVA MKEFKEEMNK KRAFIVTDKF LYNNGYIDRI EEELDHMGII HTAFYDVAPD
     PTLGCATEGA KAMESFQPDL IIAVGGGSAM DAAKIMWVMY EHPEANFKDM AMTFMDIRKR
     AYKFPKMGEK AYFCAIPTSA GTGSEVTPFA VITDEKEGVK YPLADYELLP NMAIVDADMQ
     MEMPARLTAS SGIDAMTHAL EAYVAMLRSE PADGMALKAG KTIFEYLPRS YKNGKNDSEA
     REKMAIAATM AGMAFANAFL GVCHSMAHKL GAFHHVQHGV ANALLIGQVI KYNCAEAPFK
     MGTFPQYKYP DCVERYAEFA RFCGTKPGKT DRETVDNFLV DLEKLKDEVG LPKTIKEAGV
     DEKAFLDSLD EMVLQAFNDQ CTGANPRYPL LEELKQMYLN AYYGK
//