ID Q7W715_BORPA Unreviewed; 384 AA. AC Q7W715; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 89. DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:CAE38016.1}; DE EC=1.1.1.1 {ECO:0000313|EMBL:CAE38016.1}; GN OrderedLocusNames=BPP2723 {ECO:0000313|EMBL:CAE38016.1}; OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257311 {ECO:0000313|EMBL:CAE38016.1, ECO:0000313|Proteomes:UP000001421}; RN [1] {ECO:0000313|Proteomes:UP000001421} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253 RC {ECO:0000313|Proteomes:UP000001421}; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., RA Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). 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 --------------------------------------------------------------------------- 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; BX640431; CAE38016.1; -; Genomic_DNA. DR RefSeq; WP_010928698.1; NC_002928.3. DR AlphaFoldDB; Q7W715; -. DR GeneID; 69422117; -. DR KEGG; bpa:BPP2723; -. DR HOGENOM; CLU_007207_0_0_4; -. DR Proteomes; UP000001421; Chromosome. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR CDD; cd08193; HVD; 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. PE 3: Inferred from homology; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:CAE38016.1}. FT DOMAIN 11..375 FT /note="Alcohol dehydrogenase iron-type/glycerol FT dehydrogenase GldA" FT /evidence="ECO:0000259|Pfam:PF00465" SQ SEQUENCE 384 AA; 40283 MW; 2C66450CAFDEEA91 CRC64; MNGFEFRTHA RTLAGEGTSQ RLGEAVAAQW GPCRILVVTD EQLVRLGLVA ALAQSLRDAG HTVQVYDGVL ADPPEAVVSQ AIARGRETDV QCVIGFGGGS SMDIAKLVAA FAGSAADFRD SYGIDRVATA RLPLVQVPTT AGTGSEATPI AIVTREDASK AGIVSPVLYC DIAVLDAALT RGLPPAVTAA TGIDAIVHAV EAYTSRLRKN PISDGLARQA LRLLCRSIGP ACRDGADMAA RHDMLLGAML AGQAFANAPV AAVHALAYPL GGVFHVPHGL SNALMFGAVL RFNLPQAGAA YAQLAQIACP QVDGPQQARA EGFVQEMASL GPRLGLPRRL AEVGVAERDL PMLAQQAMQQ QRLLVNNPRE LGYDDALRLY REAL //