BDH_THABB
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 03-AUG-2022, entry version 78.
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; 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=butan-1-ol + 2 Fe(III)-[cytochrome c] = butanal + 2 Fe(II)-
CC [cytochrome c] + 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}.
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DR EMBL; AF355798; AAK27220.2; -; Genomic_DNA.
DR AlphaFoldDB; Q9AF95; -.
DR SMR; Q9AF95; -.
DR KEGG; ag:AAK27220; -.
DR BioCyc; MetaCyc:MON-19863; -.
DR BRENDA; 1.1.2.9; 8965.
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 ACT_SITE 322
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 84
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 136
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 181
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 197..198
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 349
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 408..409
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 558
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 618
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 621
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 622
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 661
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
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
