ID   A0A098QZ08_9SPIO        Unreviewed;       873 AA.
AC   A0A098QZ08;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=DC28_04965 {ECO:0000313|EMBL:KGE73140.1};
OS   Spirochaeta lutea.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=1480694 {ECO:0000313|EMBL:KGE73140.1, ECO:0000313|Proteomes:UP000029692};
RN   [1] {ECO:0000313|EMBL:KGE73140.1, ECO:0000313|Proteomes:UP000029692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC230 {ECO:0000313|EMBL:KGE73140.1,
RC   ECO:0000313|Proteomes:UP000029692};
RA   Shivani Y., Subhash Y., Tushar L., Sasikala C., Ramana C.V.;
RT   "De novo Genome Sequence of Spirocheata sp.";
RL   Submitted (MAY-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:KGE73140.1}.
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DR   EMBL; JNUP01000045; KGE73140.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A098QZ08; -.
DR   STRING; 1480694.DC28_04965; -.
DR   eggNOG; COG1012; Bacteria.
DR   eggNOG; COG1454; Bacteria.
DR   Proteomes; UP000029692; 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.
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:UP000029692}.
FT   DOMAIN          6..400
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          458..855
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   873 AA;  94469 MW;  DB2427F78CD52F6F CRC64;
     MDTPKALEDL IYRVKKAQAL YATFSQDRVD EIFRRAAITA NAERIPLAKA AVAETGMGIL
     EDKVIKNHFA SEYIFNQYKD LKTCGVIESD HAFGIQKIAE PVGIICAIIP TTNPTSTAIF
     KTLIALKTRN AVIISPHPRA KGCTTQAARI VRDAAIAAGA PEDLIGWIDE PSLELSNMLM
     THGDIALILA TGGPGMVKAA YSSGKPAIGV GAGNTPALID ETADVKQAVN SILLSKTFDN
     GVICASEQSV IAHDGVYEEV REEFARRGAY VLNAEEAKAV GEVILKEGKS GKTINPEIVG
     QPAHAIAALA GISVPETAKV LIGEAQDINE NEPYAYEKLS PVLALYRCEH FEDGLSKAHE
     LVRFGGFGHT SVLYTDPVNS GRITRFGEVM KTGRVLVNMP SSQGAIGDLY NFKLAPSLTL
     GCGSWGGNAV SENVGVKHLL NIKTVAERRE NMMWFKVPPK IYHKFGCLPV ALGDLKDKKR
     VFIVTDSFLF NNGYVTKVTD TLDELGIDFQ VFHQVKPDPT LSTINAGLEN LRAFAPDVIV
     GFGGGSPMDA AKIMWLLYEH PEVTFEGLAL RFMDIEKRIY QFPDMGKKAI MVAVPTTSGT
     GSEVTPFSVV TDDKTGLKYP IADYALTPTM AIIDSSLVME MPKGLTAASG IDAVTHAIEA
     IVSVMSTDYT NGIALESLRV LFKYLPSSYR NGKTDKKARE KVHNAAAMAG MAFANAFLGV
     CHSMAHKLGA AFGIPHGVAN ALIINQTIRF NATENPTKQA AFPQYEYPSA RSRYARIAGY
     LGLAPMSAMD DPSLQDAAVE ALVKEIEALK AKLDLPHSIR AYGIDEQEFL EKVDELAEQA
     FDDQCTGANP RYPLIKEIKA MYLNAFYGKD QAV
//