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   31-JAN-2018, entry version 65.
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, ENZYME 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   -!- ENZYME 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
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}.
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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: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
//