ID N1MQL9_9SPHN Unreviewed; 581 AA.
AC N1MQL9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Quino(Hemo)protein alcohol dehydrogenase,PQQ-dependent {ECO:0000313|EMBL:CCW19211.1};
DE EC=1.1.2.- {ECO:0000313|EMBL:CCW19211.1};
GN ORFNames=EBBID32_35770 {ECO:0000313|EMBL:CCW19211.1};
OS Sphingobium indicum BiD32.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW19211.1, ECO:0000313|Proteomes:UP000013201};
RN [1] {ECO:0000313|EMBL:CCW19211.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW19211.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Le V.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW19211.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW19211.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Nielsen J.L., Zhou N.A., Kjeldal H.;
RT "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR617512-3};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR617512-3};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000256|PIRSR:PIRSR617512-2};
CC Note=Binds 1 PQQ group per subunit. {ECO:0000256|PIRSR:PIRSR617512-2};
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008156}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCW19211.1}.
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DR EMBL; CAVK010000181; CCW19211.1; -; Genomic_DNA.
DR RefSeq; WP_006962269.1; NZ_CAVK010000181.1.
DR AlphaFoldDB; N1MQL9; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000013201; Unassembled WGS sequence.
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 Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 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 NCBIfam; TIGR03075; PQQ_enz_alc_DH; 1.
DR PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR PANTHER; PTHR32303:SF20; QUINOPROTEIN ETHANOL DEHYDROGENASE; 1.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 6.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR617512-3};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR617512-4};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR617512-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CCW19211.1};
KW PQQ {ECO:0000256|ARBA:ARBA00022891, ECO:0000256|PIRSR:PIRSR617512-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000013201};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..581
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004109076"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 88
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 138
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 182
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 412..413
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT DISULFID 132..133
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 581 AA; 62304 MW; D496EB6E9E15779B CRC64;
MKGPIMRALS GVAAITLAMG AAPLVAQSGP TDADLMNDAK STGDVLTYGM GPQAHRFSSL
NAINSSNVSK MVPAFAASLG GEKQRGQEAQ PIVYDGTIYV TGSYSRLFAF DARTGEEKWQ
YDARLPDGIM PCCDVVNRGA AIYGDKIIFA TLDARLVALN RNTGKVIWNK QIADYKEGYS
ATAAPLIVNG MVITGNSGGE FGVVGAVDAR DVNTGELIWH RPVIEGHMGT LKGKDNGITG
KLNATWQGDL WKSGGGATWL GGTYDPDTNL LFFGTGNPAP WNSHLRPGDN LYTASTLAID
PATGVIKWHF QTTPHDGWDF DGVNEFIPFD ATINGKPMKL GAKADRNGYF FVLDRTNGKF
IGAHKFVMQT TWANGFNKNG KPNVIPEGRP PAPGDAKGKP VFASPSFLGG KNWMPMAYSH
DTGLFYIPSN DWGMDIWNEP IAYKKGAAYL GAGFTIKSIA DDHIGALRAM DPKTGKIMWE
YKNNAPLWGG VLTTGGNLVF TGTPEGFLKA FDAKTGQELW KFQTGSGVVG SPVTWEQDGE
QYVAVMSGWG GAVPLWGGEV AKSFKDINQG GALWVFKLPK S
//
