ID BDH_THABB Reviewed; 691 AA. AC Q9AF95; DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 2. DT 12-SEP-2018, entry version 67. DE RecName: Full=1-butanol dehydrogenase (cytochrome c) {ECO:0000303|PubMed:11238982}; DE Short=BDH {ECO:0000303|PubMed:11238982}; DE EC=1.1.2.9 {ECO:0000269|PubMed:11238982}; DE AltName: Full=NAD-independent 1-butanol dehydrogenase {ECO:0000303|PubMed:11238982}; DE AltName: Full=PQQ-containing alcohol dehydrogenase {ECO:0000303|PubMed:11889098}; DE AltName: Full=Quinohemoprotein {ECO:0000303|PubMed:11889098}; DE Flags: Precursor; GN Name=bdh {ECO:0000303|PubMed:11889098}; OS Thauera butanivorans (strain ATCC 43655 / DSM 2080/ JCM 20651 / NBRC OS 103042 / IAM 12574 / Bu B1211) (Pseudomonas butanovora). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Thauera. OX NCBI_TaxID=1219356; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, RP COFACTOR, INDUCTION, AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 43655 / DSM 2080/ JCM 20651 / NBRC 103042 / IAM 12574 / Bu RC B1211; RX PubMed=11889098; DOI=10.1128/JB.184.7.1916-1924.2002; RA Vangnai A.S., Arp D.J., Sayavedra-Soto L.A.; RT "Two distinct alcohol dehydrogenases participate in butane metabolism RT by Pseudomonas butanovora."; RL J. Bacteriol. 184:1916-1924(2002). RN [2] RP PROTEIN SEQUENCE OF 39-53, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION, SUBUNIT, RP AND SUBSTRATE SPECIFICITY. RC STRAIN=ATCC 43655 / DSM 2080/ JCM 20651 / NBRC 103042 / IAM 12574 / Bu RC B1211; RX PubMed=11238982; DOI=10.1099/00221287-147-3-745; RA Vangnai A.S., Arp D.J.; RT "An inducible 1-butanol dehydrogenase, a quinohaemoprotein, is RT involved in the oxidation of butane by Pseudomonas butanovora."; RL Microbiology 147:745-756(2001). RN [3] RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION. RC STRAIN=ATCC 43655 / DSM 2080/ JCM 20651 / NBRC 103042 / IAM 12574 / Bu RC B1211; RX PubMed=12142403; RA Vangnai A.S., Sayavedra-Soto L.A., Arp D.J.; RT "Roles for the two 1-butanol dehydrogenases of Pseudomonas butanovora RT in butane and 1-butanol metabolism."; RL J. Bacteriol. 184:4343-4350(2002). CC -!- FUNCTION: Involved in the metabolism of butane (PubMed:11889098). CC Could be important in the detoxification of 1-butanol CC (PubMed:12142403). Catalyzes the oxidation of 1-butanol to CC butyraldehyde (PubMed:11238982, PubMed:12142403). Also able to use CC 1-propanol, 2-pentanol, propionaldehyde and butyraldehyde as CC substrates (PubMed:11238982). {ECO:0000269|PubMed:11238982, CC ECO:0000269|PubMed:11889098, ECO:0000269|PubMed:12142403}. CC -!- CATALYTIC ACTIVITY: Butan-1-ol + 2 ferricytochrome c = butanal + 2 CC ferrocytochrome c + 2 H(+). {ECO:0000269|PubMed:11238982}. CC -!- COFACTOR: CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442; CC Evidence={ECO:0000269|PubMed:11238982, CC ECO:0000305|PubMed:11889098}; CC Note=Binds 1 PQQ group per subunit. {ECO:0000269|PubMed:11238982}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:11238982, CC ECO:0000305|PubMed:11889098}; CC Note=Binds 1 Ca(2+) ion per subunit. CC {ECO:0000250|UniProtKB:Q46444}; CC -!- COFACTOR: CC Name=heme c; Xref=ChEBI:CHEBI:61717; CC Evidence={ECO:0000269|PubMed:11238982}; CC Note=Binds 1 heme c group per subunit. CC {ECO:0000269|PubMed:11238982}; CC -!- ACTIVITY REGULATION: Dehydrogenase activity is increased by CC ammonium ions. {ECO:0000269|PubMed:11238982}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=7 uM for 1-butanol {ECO:0000269|PubMed:11238982}; CC KM=535 uM for butyraldehyde {ECO:0000269|PubMed:11238982}; CC pH dependence: CC Optimum pH is 8. {ECO:0000269|PubMed:11238982}; CC Temperature dependence: CC Optimum temperature is 60 degrees Celsius. CC {ECO:0000269|PubMed:11238982}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11238982}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:11889098}. CC -!- INDUCTION: By butane and 1-butanol. {ECO:0000269|PubMed:11238982, CC ECO:0000269|PubMed:11889098, ECO:0000269|PubMed:12142403}. CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a delayed CC growth on butane and are unable to tolerate high level of 1- CC butanol (PubMed:11889098, PubMed:12142403). When both bdh and boh CC genes are inactivated, growth on butane and 1-butanol is CC eliminated (PubMed:11889098). {ECO:0000269|PubMed:11889098, CC ECO:0000269|PubMed:12142403}. CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family. CC {ECO:0000305}. 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; AF355798; AAK27220.2; -; Genomic_DNA. DR ProteinModelPortal; Q9AF95; -. DR KEGG; ag:AAK27220; -. DR KO; K20936; -. DR BioCyc; MetaCyc:MONOMER-19863; -. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 1.10.760.10; -; 1. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR036909; Cyt_c-like_dom_sf. DR InterPro; IPR018391; PQQ_beta_propeller_repeat. DR InterPro; IPR017512; PQQ_MeOH/EtOH_DH. DR InterPro; IPR002372; PQQ_repeat. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR Pfam; PF13442; Cytochrome_CBB3; 1. DR Pfam; PF13360; PQQ_2; 2. DR SMART; SM00564; PQQ; 3. DR SUPFAM; SSF46626; SSF46626; 1. DR SUPFAM; SSF50998; SSF50998; 1. DR TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1. DR PROSITE; PS51007; CYTC; 1. PE 1: Evidence at protein level; KW Calcium; Direct protein sequencing; Disulfide bond; Heme; Iron; KW Metal-binding; Oxidoreductase; Periplasm; PQQ; Signal. FT SIGNAL 1 38 {ECO:0000269|PubMed:11238982, FT ECO:0000305|PubMed:11889098}. FT CHAIN 39 691 1-butanol dehydrogenase (cytochrome c). FT /FTId=PRO_0000442915. FT DOMAIN 605 684 Cytochrome c. {ECO:0000255|PROSITE- FT ProRule:PRU00433}. FT REGION 197 198 Pyrroloquinoline quinone binding. FT {ECO:0000250|UniProtKB:Q46444}. FT REGION 408 409 Pyrroloquinoline quinone binding. FT {ECO:0000250|UniProtKB:Q46444}. FT ACT_SITE 322 322 Proton acceptor. FT {ECO:0000250|UniProtKB:Q46444}. FT METAL 199 199 Calcium. {ECO:0000250|UniProtKB:Q46444}. FT METAL 322 322 Calcium. {ECO:0000250|UniProtKB:Q46444}. FT METAL 622 622 Iron (heme axial ligand); via tele FT nitrogen. {ECO:0000250|UniProtKB:Q46444}. FT METAL 661 661 Iron (heme axial ligand). FT {ECO:0000250|UniProtKB:Q46444}. FT BINDING 84 84 Pyrroloquinoline quinone. FT {ECO:0000250|UniProtKB:Q46444}. FT BINDING 136 136 Pyrroloquinoline quinone. FT {ECO:0000250|UniProtKB:Q46444}. FT BINDING 181 181 Pyrroloquinoline quinone. FT {ECO:0000250|UniProtKB:Q46444}. FT BINDING 349 349 Pyrroloquinoline quinone. FT {ECO:0000250|UniProtKB:Q46444}. FT BINDING 558 558 Pyrroloquinoline quinone; via amide FT nitrogen. {ECO:0000250|UniProtKB:Q46444}. FT BINDING 618 618 Heme c (covalent). FT {ECO:0000250|UniProtKB:Q46444}. FT BINDING 621 621 Heme c (covalent). FT {ECO:0000250|UniProtKB:Q46444}. FT DISULFID 130 131 {ECO:0000250|UniProtKB:Q46444}. SQ SEQUENCE 691 AA; 75071 MW; 4FC7FD20CDA14E64 CRC64; MLTTTFARKR EESVPLRKGI QRALLGLSCL VLSTTSFAAG GEWRTHGYDD AGTRYSPLAQ ITPDNAKELG LVWSYDLESS RGVEATPIVV DGVMYVTAPW SVVHALDVRS GKRLWTYDPE VPREKGKNAC CDVVNRGVAV HEGKVFVGSL DGRLVAIDAR TGKRVWERNT LIDDDKPYTI TGAPRVIKGK VVIGNGGAEF GVRGYITAYD PTAASRPGVV PGPGDPSLPF EDASMEAAAK TWDPAGQVLG SGRRRHGVEL DGLYRKAGFC CTSAPATPSP WSHRKRSPAG GDNLYTASIV ALRPDTGEYV WHYQQTPADN WDYTSTQDLI LADIELGGKP RKVILHAPKN GFFFVIDRTD GKFISAQNFV PVNWATGYDE NGRPIENPEG AWPGHLSMRF PAPSARTNWH SMSYSPQTGL AYFPAQNIPL VLQEDKNWSY NQAQPGQAMA GIGWNLGMLV NPRPPASQPF GRLIAWDPVQ QKEVWRKEHV SPWNGGTLVT AGNVVFQGTA DARLLAFDAR DGKELWSAPM GTGVIAAPVT YEVDGKQYVS IAVGWGGVYG NFTRASERRT PGTVYTFALG GKAEMPAFTE YQLNNLVSGV DYNPDDVAEG TGLYVTNCVF CHGVPGVDKG GGIPNLGYST AETIAHLDQF VFKGPFMPRG MPDFTGKLTP EQVEKIKAFI LGTADAVRPK K //