ID A0A1E5D0V5_9VIBR Unreviewed; 415 AA.
AC A0A1E5D0V5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OEE76997.1};
GN ORFNames=A130_14955 {ECO:0000313|EMBL:OEE76997.1};
OS Vibrio genomosp. F6 str. FF-238.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1191298 {ECO:0000313|EMBL:OEE76997.1, ECO:0000313|Proteomes:UP000094165};
RN [1] {ECO:0000313|EMBL:OEE76997.1, ECO:0000313|Proteomes:UP000094165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FF-238 {ECO:0000313|EMBL:OEE76997.1,
RC ECO:0000313|Proteomes:UP000094165};
RX PubMed=22955834; DOI=10.1126/science.1219385;
RA Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA Le Roux F., Mincer T., Polz M.F.;
RT "Ecological populations of bacteria act as socially cohesive units of
RT antibiotic production and resistance.";
RL Science 337:1228-1231(2012).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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:OEE76997.1}.
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; AJYW02000097; OEE76997.1; -; Genomic_DNA.
DR RefSeq; WP_017054616.1; NZ_AJYW02000097.1.
DR AlphaFoldDB; A0A1E5D0V5; -.
DR Proteomes; UP000094165; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd08189; Fe-ADH-like; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF102; ALCOHOL DEHYDROGENASE 4; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000094165}.
FT DOMAIN 30..388
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 415 AA; 44842 MW; 35C166E989529CB6 CRC64;
MPTQIQLFGY KSYMKALKVA AKVIPMPKPT LFTGVGSSIE LCEAISLIGI KKLLLVTDES
IVRLGLLKPI QQALQDSGVE MAIFSQVQPD PTYLQVEAGL RIYLRCECDG ILAVGGGSPI
DTAKVIAAKV HNPKPIHKLA GLFRVWKTPA PLFAIPTTAG TGSEVTIAAV VSDPDSHQKT
PLIDPKLVPM MAALDPSIMV GLPRPITAAT GMDALTHAIE SYLSMNATNE TNGYALAAVK
LVMTNLPLAY ENGENLVARQ NMAIASYYAG LAFTKASLGY VHAISHNLGA LYGVPHGLAN
AIVLPYVLDF SQHATQPQLA ELFRATSNSN EEMSESEQAQ AFIQLVRQLQ QQLKIPATLD
MLVENDISHL AKLALKEAHH NYPVPVYMGK KQCEQLLRSM MTPVTVMDEA LPEPK
//
