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Database: UniProt
Entry: H1SCA5_9BURK
LinkDB: H1SCA5_9BURK
Original site: H1SCA5_9BURK 
ID   H1SCA5_9BURK            Unreviewed;       574 AA.
AC   H1SCA5;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Pyrrolo-quinoline quinone {ECO:0000313|EMBL:EHP39883.1};
GN   ORFNames=OR16_29204 {ECO:0000313|EMBL:EHP39883.1};
OS   Cupriavidus basilensis OR16.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP39883.1, ECO:0000313|Proteomes:UP000005808};
RN   [1] {ECO:0000313|EMBL:EHP39883.1, ECO:0000313|Proteomes:UP000005808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR16 {ECO:0000313|EMBL:EHP39883.1,
RC   ECO:0000313|Proteomes:UP000005808};
RX   PubMed=22461549; DOI=10.1128/JB.06752-11;
RA   Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA   Nagy I., Horvath B., Nagy I., Kukolya J.;
RT   "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL   J. Bacteriol. 194:2109-2110(2012).
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:EHP39883.1}.
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DR   EMBL; AHJE01000081; EHP39883.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1SCA5; -.
DR   PATRIC; fig|1127483.3.peg.5828; -.
DR   Proteomes; UP000005808; Unassembled WGS sequence.
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; PF01011; PQQ; 1.
DR   Pfam; PF13360; PQQ_2; 1.
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..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..574
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012926416"
FT   ACT_SITE        311
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         75
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         125
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         169
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         187
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         269
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         311
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   DISULFID        119..120
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   574 AA;  61976 MW;  9D6F65C35FCBA0F0 CRC64;
     MMVLAATAAS LAAQAAVTDA MIENDAKSPG DVLSWGMGTQ GQRFSTLNRI NTKNISQLVP
     AWSFSFGGEK QRGQEAQPLI HEGKMFVTAS YSRIYALDLK TGSKLWKYEH RLPEGIMPCC
     DVVNRGAALY DNLVIFGTLD AQLVALDQKT GKVVWKDKIE DYAAGYSYTA APLIVKGMVL
     TGISGGEFGV VGRVEARDAK TGQMVWSRPV VEGHMGYTYD KDGNKTENGV TGTLNASWPG
     ETWKTGGAAT WLGGTYDPKT GLAYFGTGNP GPWNSHMRKG DNLYSASTVA LDPATGKIVW
     HYQNTPNDGW DFDGVNEFVT FDQDGKRLGG KADRNGFFYV NDATTGKLVN AFPFVKKITW
     ASSIDLKTGR PNMIAQSRPG DPAAGSDPKK GQSVFAAPGF LGGKNQQPMA YSPQTGLFYV
     PANEWGMDIW NEPVSYKKGA AFLGAGFTIH PLNEDYIGSL RAINPKTGKI EWEVKNYAPL
     WGGVMTTAGG LVFWGTPEGY LKAADAKTGK ELWKFQTGSG VVAPPVTWEE GGEQYVAVVS
     GWGGAVPLWG GEVAKRVNFL EQGGSVWVFK LHKS
//
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