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XOXF_PARDE
ID   XOXF_PARDE              Reviewed;         600 AA.
AC   P29968;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative dehydrogenase XoxF;
DE            EC=1.1.99.-;
DE   Flags: Precursor;
GN   Name=xoxF;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Harms N.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 380-600.
RC   STRAIN=Pd 1235;
RX   PubMed=1657873; DOI=10.1128/jb.173.21.6971-6979.1991;
RA   Ras J., Reijnders W.N.M., van Spanning R.J.M., Harms N., Oltmann L.F.,
RA   Stouthamer A.H.;
RT   "Isolation, sequencing, and mutagenesis of the gene encoding cytochrome
RT   c553i of Paracoccus denitrificans and characterization of the mutant
RT   strain.";
RL   J. Bacteriol. 173:6971-6979(1991).
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 PQQ group per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U34346; AAC44555.1; -; Genomic_DNA.
DR   EMBL; M75583; AAA25574.1; -; Genomic_DNA.
DR   PIR; A41378; A41378.
DR   AlphaFoldDB; P29968; -.
DR   SMR; P29968; -.
DR   PRIDE; P29968; -.
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   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; PF13360; PQQ_2; 1.
DR   SMART; SM00564; PQQ; 5.
DR   SUPFAM; SSF50998; SSF50998; 1.
DR   TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1.
DR   PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE   3: Inferred from homology;
KW   Calcium; Metal-binding; Oxidoreductase; PQQ; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..600
FT                   /note="Putative dehydrogenase XoxF"
FT                   /id="PRO_0000025564"
FT   ACT_SITE        318
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   600 AA;  65159 MW;  DCA996F1BCC5A3CE CRC64;
     MKNLMNGACL ALLMSGTAAL ANEQRAGRDR QAPQWAIQMG DYANTRYSTL DQINKDNVKD
     LRVAWTFSTG VLRGHEGSPL VIGDVMYVHT PFPNRVFALD LNDNGKILWR YEPQQDPNVI
     AVMSCDTVYR GLSYADGMIL LGQADTTVVA LDATSGEVKW STKIGDPGIG ETLTATVVPV
     KDKVLVGISG GEYGVRGRMT ALNLTDGSEA WKAWSTGPDE ELLVDPETTT HLGKPIGADS
     SLNSWEGDQW QIGGGTIWGW FSYDPDLNLV YYGTGNPSTW NPSQRPGDNK WSMTIMARDA
     DTGMAKWFYQ MTPHDEWDYD GVNEMILTNQ TVDGQERKLL THFDRNGLAY TMDRETGELL
     VAEKYDPVVN WTTGVDMDPN SETYGRPAVV AEYSTAQNGE DENTTGVCPA ALGTKDQQPA
     AFSPKTNLFY VPTNHVCMDY EPFRVAYTAG QPYVGATLSM YPAPNSHGGM GNFIAWHNTT
     GEIKWSVPEQ FSVWSGALAT AGDVVFYGTL EGYLKPVDAQ TGEELYKFKT PSGIIGNVMT
     YEHGGKQYVG ILSGVGGWAG IGLAAGLTNP NDGLGAVGGY ASLSQYTELG GQLTVFELPG
 
 
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