ID   E8LNQ2_9VIBR            Unreviewed;       899 AA.
AC   E8LNQ2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=VIBR0546_07722 {ECO:0000313|EMBL:EGA67664.1};
OS   Vibrio brasiliensis LMG 20546.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=945543 {ECO:0000313|EMBL:EGA67664.1, ECO:0000313|Proteomes:UP000004371};
RN   [1] {ECO:0000313|EMBL:EGA67664.1, ECO:0000313|Proteomes:UP000004371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20546 {ECO:0000313|EMBL:EGA67664.1,
RC   ECO:0000313|Proteomes:UP000004371};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EGA67664.1}.
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DR   EMBL; AEVS01000006; EGA67664.1; -; Genomic_DNA.
DR   RefSeq; WP_006877464.1; NZ_AEVS01000006.1.
DR   AlphaFoldDB; E8LNQ2; -.
DR   STRING; 945543.VIBR0546_07722; -.
DR   eggNOG; COG1012; Bacteria.
DR   eggNOG; COG1454; Bacteria.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000004371; 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}.
FT   DOMAIN          4..354
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          458..848
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   899 AA;  97112 MW;  7027431E53CB9A99 CRC64;
     MPVTNMAELD AMIARVKKAQ EEFATYSQEQ VDKIFRAASL AANQARIPLA QQAVEESGMG
     IVEDKVIKNH FASEFIYNKY KDEQTCGILE EDDNLGTMTI AEPVGIICGI VPTTNPTSTA
     IFKSLISLKT RNGIIFSPHP RAKNSTNDAA KLVLDAAVAA GAPKDIIGWI DQPSVELSNA
     LMKHDDIALI LATGGPGMVK AAYSSGKPAI GVGAGNVPVV IDETADIKRA VASILMSKTF
     DNGVVCASEQ AAIVVDEVYD EVKERFASHK AYVLSKAEAE KVRKVLLIDG ALNAKIVGQP
     APAIAEMAGV KVPADTKVLV GEGLGKVSYD DAFAHEKLSP TLGLFRADNF EDAVAQAVTM
     VEIGGIGHTS GLYTNQDVNA DRIRYFGDKM KTARILINIP TTHGGIGDLY NFNVAPSLTL
     GCGSWGGNSI SENVGPKHLI NKKTVAKRAE NMLWHKLPKS IYFRRGSLPI ALSDLEGKKR
     AFLVTDRFLF NNGYADDVVS LLKAQGMEVQ TFFDVEADPT LSVVEKGAEA MKSFQPDTII
     ALGGGSPMDA AKIMWVMYEH PETHFEELAM RFMDIRKRIY KFPKMGKKAE LVCITTTSGT
     GSEVTPFAVV TDDKTGAKYP LADYEITPNM AIVDANLVMN MPKSLTAFGG YDAVTHALEA
     YVSVLANEYS DGQALQALKM LKEYLPSSYA NGANDPIARE KVHNAATIAG VAFANAFLGV
     CHSMAHKIGA EFHLPHGLAN ALLISNVVRY NANDNPTKQT AFSQYDRPQA RRRYAEVADH
     LGLSQEGDRT AQKIERLLAW LDELKANLDI PMSIQAAGVS EADFVAKLDE LAVEAFDDQC
     TGANPRYPLI AELKEVLLAS YYGKAFVEGE TFEGTTVIKK KADQVAKEAP KAKKAKAEA
//