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 02-DEC-2020, entry version 73. 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 103042 OS / IAM 12574 / Bu B1211) (Pseudomonas butanovora). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae; OC 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 by RT Pseudomonas butanovora."; RL J. Bacteriol. 184:1916-1924(2002). RN [2] RP PROTEIN SEQUENCE OF 39-53, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND SUBSTRATE RP 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 involved in RT 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; DOI=10.1128/jb.184.16.4343-4350.2002; RA Vangnai A.S., Sayavedra-Soto L.A., Arp D.J.; RT "Roles for the two 1-butanol dehydrogenases of Pseudomonas butanovora in RT butane and 1-butanol metabolism."; RL J. Bacteriol. 184:4343-4350(2002). CC -!- FUNCTION: Involved in the metabolism of butane (PubMed:11889098). Could CC be important in the detoxification of 1-butanol (PubMed:12142403). CC Catalyzes the oxidation of 1-butanol to butyraldehyde (PubMed:11238982, CC PubMed:12142403). Also able to use 1-propanol, 2-pentanol, CC propionaldehyde and butyraldehyde as substrates (PubMed:11238982). CC {ECO:0000269|PubMed:11238982, ECO:0000269|PubMed:11889098, CC ECO:0000269|PubMed:12142403}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 [Fe(III)cytochrome c] + butan-1-ol = 2 [Fe(II)cytochrome c] CC + butanal + 2 H(+); Xref=Rhea:RHEA:43432, Rhea:RHEA-COMP:10350, CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:15743, CC ChEBI:CHEBI:28885, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.1.2.9; CC Evidence={ECO:0000269|PubMed:11238982}; CC -!- COFACTOR: CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442; CC Evidence={ECO:0000269|PubMed:11238982, 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, ECO:0000305|PubMed:11889098}; CC Note=Binds 1 Ca(2+) ion per subunit. {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. {ECO:0000269|PubMed:11238982}; CC -!- ACTIVITY REGULATION: Dehydrogenase activity is increased by ammonium CC 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 growth on CC butane and are unable to tolerate high level of 1-butanol CC (PubMed:11889098, PubMed:12142403). When both bdh and boh genes are CC inactivated, growth on butane and 1-butanol is eliminated CC (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 SMR; Q9AF95; -. DR KEGG; ag:AAK27220; -. 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 FT /evidence="ECO:0000269|PubMed:11238982, FT ECO:0000305|PubMed:11889098" FT CHAIN 39..691 FT /note="1-butanol dehydrogenase (cytochrome c)" FT /id="PRO_0000442915" FT DOMAIN 605..684 FT /note="Cytochrome c" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT REGION 197..198 FT /note="Pyrroloquinoline quinone binding" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT REGION 408..409 FT /note="Pyrroloquinoline quinone binding" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT ACT_SITE 322 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT METAL 199 FT /note="Calcium" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT METAL 322 FT /note="Calcium" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT METAL 622 FT /note="Iron (heme axial ligand); via tele nitrogen" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT METAL 661 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT BINDING 84 FT /note="Pyrroloquinoline quinone" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT BINDING 136 FT /note="Pyrroloquinoline quinone" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT BINDING 181 FT /note="Pyrroloquinoline quinone" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT BINDING 349 FT /note="Pyrroloquinoline quinone" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT BINDING 558 FT /note="Pyrroloquinoline quinone; via amide nitrogen" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT BINDING 618 FT /note="Heme c (covalent)" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT BINDING 621 FT /note="Heme c (covalent)" FT /evidence="ECO:0000250|UniProtKB:Q46444" FT DISULFID 130..131 FT /evidence="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 //