GenomeNet

Database: UniProt
Entry: A5W502_PSEP1
LinkDB: A5W502_PSEP1
Original site: A5W502_PSEP1 
ID   A5W502_PSEP1            Unreviewed;       595 AA.
AC   A5W502;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Pyrrolo-quinoline quinone {ECO:0000313|EMBL:ABQ79212.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Pput_3084 {ECO:0000313|EMBL:ABQ79212.1};
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ79212.1};
RN   [1] {ECO:0000313|EMBL:ABQ79212.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F1 {ECO:0000313|EMBL:ABQ79212.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000712; ABQ79212.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5W502; -.
DR   KEGG; ppf:Pput_3084; -.
DR   eggNOG; COG4993; Bacteria.
DR   HOGENOM; CLU_018478_0_0_6; -.
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   PQQ {ECO:0000256|ARBA:ARBA00022891, ECO:0000256|PIRSR:PIRSR617512-2};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..595
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002687621"
FT   ACT_SITE        323
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         137
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         199
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         281
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         323
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         417..418
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   DISULFID        131..132
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   595 AA;  64884 MW;  E2DC13AE1A002501 CRC64;
     MTRSPRRPLF AVSLVLSAML LAGAAHAAVS NEEILQDPKN PQQIVTNGLG VQGQRYSPLD
     LLNVNNVKEL RPVWAFSFGG EKQRGQQAQP LIKDGVMYLT GSYSRVFAVD ARTGKKLWQY
     DARLPDDIRP CCDVINRGVA LYGNLVFFGT LDAKLVALNK DTGKVVWSKK VADHKEGYSI
     SAAPMIVNGK LITGVAGGEF GVVGKIQAYN PENGELLWMR PTVEGHMGYV YKDGKAIENG
     ISGGEAGKTW PGDLWKTGGA APWLGGYYDP ETNLILFGTG NPAPWNSHLR PGDNLYSSSR
     LALNPDDGTI KWHFQSTPHD GWDFDGVNEL ISFNYKDGGK EIKAAATADR NGFFYVLDRT
     NGKFIRGFPF VDKITWATGL DKDGRPIYND ASRPGAPGSE AKGSSVFVAP AFLGAKNWMP
     MAYNKDTGLF YVPSNEWGMD IWNEGIAYKK GAAFLGAGFT IKPLNEDYIG VLRAIDPISG
     KEVWRHKNYA PLWGGVLTTK GNLVFTGTPE GFLQAFNAKT GDKVWEFQTG SGVLGSPVTW
     EMDGEQYVSV VSGWGGAVPL WGGEVAKRVK DFNQGGMLWT FKLPKQLQQT ASAKP
//
DBGET integrated database retrieval system