BOH_THABB
ID BOH_THABB Reviewed; 623 AA.
AC Q9AGW3;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=1-butanol dehydrogenase (quinone) {ECO:0000303|PubMed:12142403};
DE EC=1.1.5.11 {ECO:0000269|PubMed:12142403, ECO:0000305|PubMed:11889098};
DE AltName: Full=PQQ-containing alcohol dehydrogenase {ECO:0000303|PubMed:11889098};
DE AltName: Full=Quinoprotein alcohol dehydrogenase {ECO:0000303|PubMed:11889098};
DE Flags: Precursor;
GN Name=boh {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, CATALYTIC ACTIVITY, COFACTOR,
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION.
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, INDUCTION, AND SUBSTRATE SPECIFICITY.
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). May
CC function primarily in energy generation (PubMed:12142403). Catalyzes
CC the oxidation of 1-butanol to 1-butanal (PubMed:11889098,
CC PubMed:12142403). Also able to use 2-butanol and butyraldehyde,
CC although the affinity is comparatively low (PubMed:12142403).
CC {ECO:0000269|PubMed:11889098, ECO:0000269|PubMed:12142403}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + butan-1-ol = a quinol + butanal;
CC Xref=Rhea:RHEA:49808, ChEBI:CHEBI:15743, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:28885, ChEBI:CHEBI:132124; EC=1.1.5.11;
CC Evidence={ECO:0000269|PubMed:12142403, ECO:0000305|PubMed:11889098};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000305|PubMed:11889098};
CC Note=Binds 1 PQQ group per subunit. PQQ is inserted between disulfide
CC Cys-134-Cys-135 and the plane of Trp-277.
CC {ECO:0000250|UniProtKB:Q9Z4J7};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000305|PubMed:11889098};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q9Z4J7};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 uM for 1-butanol {ECO:0000269|PubMed:12142403};
CC KM=369 uM for butyraldehyde {ECO:0000269|PubMed:12142403};
CC KM=662 uM for 2-butanol {ECO:0000269|PubMed:12142403};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:11889098}.
CC -!- INDUCTION: By butane, 1-butanol and 2-butanol.
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; AF326086; AAK15506.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AGW3; -.
DR SMR; Q9AGW3; -.
DR KEGG; ag:AAK15506; -.
DR BioCyc; MetaCyc:MON-19862; -.
DR BRENDA; 1.2.5.2; 8965.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR CDD; cd10277; PQQ_ADH_I; 1.
DR InterPro; IPR034119; ADHI.
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 InterPro; IPR001479; Quinoprotein_DH_CS.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 4.
DR SUPFAM; SSF50998; SSF50998; 1.
DR TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Metal-binding; Oxidoreductase; Periplasm; PQQ;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..623
FT /note="1-butanol dehydrogenase (quinone)"
FT /id="PRO_5004323986"
FT REGION 235..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 90
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 140
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 184
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 202..204
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 374
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 592
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT DISULFID 134..135
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
SQ SEQUENCE 623 AA; 67553 MW; A573A1C64AC12D55 CRC64;
MKKSHAKPFA LRAIVVATAA ALSLPAAAVT DVTWEDIAND HKTTGDVLTY GLGLKAQRHS
PLKAINTDNV ANLVPAWSFS FGGEKQRGQE AQVLVHDGVI YATASYSRIF AIDARSGKRL
WEYNARLPDD IRPCCDVVNR GAAIYGDKVF FGTLDAAMVA LDRKTGKVVW RKKFGDHKVG
YTMTGAPFVI KDQKSGRTLL VHGSSGDEFG VVGWLFARDP DTGEEVWARP MVEGHMGRLN
GKDSTPTGDP KAPSWPDDPN SPTGKVEAWS QGGGAPWQTA SFDVENNMVV IGAGNPAPWN
TWKRTAPGDD PRNWDSLFTS GQAYVDASTG ELKGFYQHTP NDAWDFSGNN SVVLFEYKDP
KTGKMVNASA HADRNGFFFV TDRDMLAKGA GYPNKPTSLI GAWPFVDGIT WASGFDLKTG
KPIEKDNRPP QPKEGADKGE SIFVSPPFLG GTNWHPMSYS PDTGLFYIPA NHWAMDYWTE
NVTYKAGSAY LGQGFRIKNL FDDHVGILRA IDPSPARSLG AQGRVPAVAG TLTTAGGWVF
TGTSDGYLKA FDAKNGKELW KFQTGSGVVS VPVTWEMDGE QYVAIQSGYG GAVPLWGGDM
AELTKQVTQG GSMWVFKLPK ASR
