ID Q470N4_CUPPJ Unreviewed; 580 AA.
AC Q470N4;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Pyrrolo-quinoline quinone {ECO:0000313|EMBL:AAZ61149.1};
GN OrderedLocusNames=Reut_A1784 {ECO:0000313|EMBL:AAZ61149.1};
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ61149.1};
RN [1] {ECO:0000313|EMBL:AAZ61149.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JMP134 {ECO:0000313|EMBL:AAZ61149.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Chromosome1 of Ralstonia eutropha JMP134.";
RL Submitted (AUG-2005) 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}.
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DR EMBL; CP000090; AAZ61149.1; -; Genomic_DNA.
DR AlphaFoldDB; Q470N4; -.
DR STRING; 264198.Reut_A1784; -.
DR KEGG; reu:Reut_A1784; -.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_0_0_4; -.
DR OrthoDB; 9794322at2; -.
DR GO; GO:0016020; C:membrane; 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 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; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 6.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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 PQQ {ECO:0000256|PIRSR:PIRSR617512-2}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..580
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004232940"
FT REGION 375..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 81
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 131
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 175
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT DISULFID 125..126
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 580 AA; 62605 MW; 92C89CE3992881C7 CRC64;
MRTLRLMMAV ATAVASLATQ AAVTDAMIEN DAKSPGDVLS WGMGPQGQRY SGLTRINTKN
VGNLVPAWSF SFGGEKQRGQ EAQPLIHDGK MFVTASYSRI YALDLKTGSK LWKYEHRLPE
GIMPCCDVVN RGAALYDNLV IFGTLDAQLV ALDQKTGKVV WKEKLEDYAA GYSYTAAPLI
VKGMVLTGIS GGEFGVVGRV EARDAKTGQL VWSRPVVEGH MGYKYDKDGN KTENGVTGTE
NASWPGETWK TGGAATWLGG TYDPATGLAY FGTGNPGPWN SHIRKGDNLY SASTVAIDPA
TGKIVWHYQN TPNDGWDFDG VNEFVTFDLD GKRMGGKADR NGFFYVNDAT NGKLVNAFPF
VKKITWATGI DLKTGRPTFN DEGRPGDPAS GADPKKGKSV FAAPGFLGGK NQQPMAYSPQ
TGLFYVPANE WGMDIWNEPV SYKKGAAFLG AGFTIHPLNE DYIGSLRAIN PKTGKIVWEV
KNNAPLWGGV MTTAGGLVFW GTPEGYLKAA DARTGKELWK FQTGSGVVAP PVTWEENGEQ
YVAVVSGWGG AVPLWGGEVA KRVNFLEQGG SVWVFKLHKG
//
