ID   S5QV85_9STRE            Unreviewed;       893 AA.
AC   S5QV85;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=KE3_0170 {ECO:0000313|EMBL:AGS04752.1};
OS   Streptococcus lutetiensis 033.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1076934 {ECO:0000313|EMBL:AGS04752.1, ECO:0000313|Proteomes:UP000015268};
RN   [1] {ECO:0000313|EMBL:AGS04752.1, ECO:0000313|Proteomes:UP000015268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=033 {ECO:0000313|EMBL:AGS04752.1,
RC   ECO:0000313|Proteomes:UP000015268};
RX   PubMed=23782707; DOI=10.1186/1471-2180-13-141;
RA   Jin D., Chen C., Li L., Lu S., Li Z., Zhou Z., Jing H., Xu Y., Du P.,
RA   Wang H., Xiong Y., Zheng H., Bai X., Sun H., Wang L., Ye C., Gottschalk M.,
RA   Xu J.;
RT   "Dynamics of fecal microbial communities in children with diarrhea of
RT   unknown etiology and genomic analysis of associated Streptococcus
RT   lutetiensis.";
RL   BMC Microbiol. 13:141-141(2013).
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; CP003025; AGS04752.1; -; Genomic_DNA.
DR   RefSeq; WP_020916089.1; NC_021900.1.
DR   AlphaFoldDB; S5QV85; -.
DR   GeneID; 58527587; -.
DR   KEGG; slu:KE3_0170; -.
DR   PATRIC; fig|1076934.5.peg.173; -.
DR   HOGENOM; CLU_007207_1_0_9; -.
DR   Proteomes; UP000015268; 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.
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          25..284
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          472..882
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   893 AA;  97503 MW;  8ED2B13AB032C60A CRC64;
     MAKATNADVK NNELIAEELA QQYTGALVEK ALEAERVYAT YSQEQVDNIV AAMALAGSEA
     SLELAKEAHT ETGRGVVEDK DIKNHFATEY VYERIKNEKT VGIIGEDKVS GSIQIAAPLG
     VLAGIVPTTN PTSTTMFKIL VALKTRNAIV FAFHPQAQNC SAHAAQILYD AAIKAGAPEN
     IVQWIETPSL ANTSALIQNP KIASILATGG PGMVNAALKS GNPSMGVGAG NGAIYVDATA
     HVDRAVEDLL LSKRFDNGMI CATENSAVVE APIYDEWLQK MQDKGAYLVP EKDYKKLEDF
     VFNDRHGVNG PVAGMPARWI CEQAGVKLPE GKDVLLFELD KKNIGEKLSS EKLSPLLSVY
     KAKDRAEGVE IVEALLDYQG AGHNAGIQIG SQADPFVAEY GDAVKASRVL VNQPDSVGGI
     GDIYTDALKA SLTLGTGSWG KNSLSHNLST GDLLNVKTVA KRRNRPQWIR LPEKTYYEKN
     AISYLQDEYE PMQRALIVAD PGMVQFGFVD TVLAQLALRD EKVATSIYGT IKPDPTLGQT
     IEIAKQMRDF KPDTVIAVGG GSALDAAKIA RYIYEYSLDQ EADFLDSYEN VSELFLRLQQ
     KFIDIRKRIV KFKHQTATRL FCIPTTSGTG SEVTPYAVIT DDHTHVKYPL TDYELTPQVA
     IVDPEFVMTV PKRTVALSGL DTLSHALEAY VSVMASDLTR PWSLEAIKLV IENLEDSYNY
     DPKHPTLRGE QARENMHYAA TLAGMAFSNA FLGINHSIAH KTGGEFGLPH GLAISIAMQH
     VIRYNGVAGN VKRSVFPRYE EYRAQRDYAD IARSLDLKGK DDAALVEALC ERIDALMKAV
     DVDPRLSANG VTKEAFDAAV DKLASLAYDD QCTPANPRQP YISELKQLLI DMF
//