ID   F9TCN0_9VIBR            Unreviewed;       900 AA.
AC   F9TCN0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN   ORFNames=IX91_10630 {ECO:0000313|EMBL:AIW14652.1};
OS   Vibrio tubiashii ATCC 19109.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=1051646 {ECO:0000313|EMBL:AIW14652.1, ECO:0000313|Proteomes:UP000030071};
RN   [1] {ECO:0000313|EMBL:AIW14652.1, ECO:0000313|Proteomes:UP000030071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19109 {ECO:0000313|EMBL:AIW14652.1,
RC   ECO:0000313|Proteomes:UP000030071};
RA   Richards G.P., Needleman D.S., Watson M.A., Bono J.L.;
RT   "First Complete Genome Sequence of the Shellfish Pathogen Vibrio
RT   tubiashii.";
RL   Submitted (AUG-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   ---------------------------------------------------------------------------
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; CP009354; AIW14652.1; -; Genomic_DNA.
DR   RefSeq; WP_004748499.1; NZ_CP009354.1.
DR   AlphaFoldDB; F9TCN0; -.
DR   STRING; 1051646.IX91_10630; -.
DR   KEGG; vtu:IX91_10630; -.
DR   PATRIC; fig|1051646.9.peg.2112; -.
DR   eggNOG; COG1012; Bacteria.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_2_1_6; -.
DR   Proteomes; UP000030071; Chromosome 1.
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..401
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   900 AA;  96686 MW;  0165E463F3266898 CRC64;
     MPVTNMAELD AMVARVKAAQ AEFATFSQEK VDAIFRAASL AANHARIPLA QQAVEESGMG
     IVEDKVIKNH FASEFIYNKY KDEKTCGILE EDDNLGTMTI AEPVGIICGI VPTTNPTSTA
     IFKSLISLKT RNGIIFSPHP RAKNSTNDAA KLVLDAAVAA GAPKDIIGWI DQPSVELSNG
     LMKHDDIALI LATGGPGMVK AAYSSGKPAI GVGAGNVPVV IDETADVKRA VASILMSKTF
     DNGVVCASEQ AAIVVDEVYD EVKERFATHK AVVLSKADAD KVRKVLLIDG ALNAKIVGQP
     AAAIAELAGV KVPADTKVLV GEGLGKVSYD DAFAHEKLSP TLGLFRADDF EDAVAQAVTM
     VEIGGIGHTS GLYTNQDTNA DRIRYFGDKL KTARILVNIP TTHGGIGDLY NFNVAPSLTL
     GCGSWGGNSI SENVGPKHLI NKKTVAKRAE NMLWHKLPKS IYFRRGSLPI ALGDLEGKKR
     AFLVTDRFLF NNGYADEVVK LLKAQGIEVQ VFFDVEADPT LSVVEKGAEA MKSFQPDVIL
     ALGGGSPMDA AKIMWVMYEH PETHFAELAM RFMDIRKRIY KFPKMGKKAE LVCITTTSGT
     GSEVTPFAVV TDDKTGAKYP LADYEITPNM AIVDANLVMN MPKSLTAFGG YDAVTHALEA
     YVSVLANEYS DGQALQALKM LKEYLPSSYA NGANDPIARE KVHNAATIAG VAFANAFLGV
     CHSMAHKIGA EFHLPHGLAN ALLISNVVRY NANDNPTKQT AFSQYDRPQA RRRYAEVADH
     LGLSQAGDRT AQKIERLLAW LDELKGNLDI PMSIQAAGVS EADFVAKLDE LAVEAFDDQC
     TGANPRYPLI TELKEVLLAS YYGKAFVEGE TFEGTTVIKK KADQEAAKAA PKAKKAKAEA
//