ID Q5R120_IDILO Unreviewed; 382 AA.
AC Q5R120;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AAV81636.1};
GN OrderedLocusNames=IL0796 {ECO:0000313|EMBL:AAV81636.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV81636.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV81636.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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}.
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DR EMBL; AE017340; AAV81636.1; -; Genomic_DNA.
DR RefSeq; WP_011234047.1; NC_006512.1.
DR AlphaFoldDB; Q5R120; -.
DR STRING; 283942.IL0796; -.
DR KEGG; ilo:IL0796; -.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_0_0_6; -.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000001171; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd08188; PDDH; 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; PS00913; ADH_IRON_1; 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:UP000001171}.
FT DOMAIN 11..374
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 382 AA; 40430 MW; 55BBF6BC4EFE8A6C CRC64;
MSSTFYIPAV NIIGENALKD AATQMDNYGF KQALIVTDPG MTKLGVTAEI EALLKEHGID
SLIYDGVQPN PTVTNVKAGL DVLQKHQCDC VISLGGGSAH DCAKGIALVA TNGGHISDYE
GVDVSKKPQL PLISINTTAG TASEMTRFCI ITDPERHIKM AIVDQNVTPI LSVNDPRLMV
GMPASLTAAT GMDALTHAVE AYVSTDATPI TDACAIKAIE IIRDNLHEAV HNGANMEARE
QMAYAQFLAG MAFNNASLGY VHAMAHQLGG FYDLPHGVCN AVLLPHVQRY NSQVVAPRLK
DIGKALGAEV QGLTEKEGAD AAIAAIVKLS QSVNIPAGLE ELGAKEEDFN TLADNAMKDA
CGLTNPIQPS HEDIVTIFKA AF
//
