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Database: UniProt
Entry: J2FVJ8_9SPHN
LinkDB: J2FVJ8_9SPHN
Original site: J2FVJ8_9SPHN 
ID   J2FVJ8_9SPHN            Unreviewed;       810 AA.
AC   J2FVJ8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0000313|EMBL:EJL21190.1};
GN   ORFNames=PMI02_05261 {ECO:0000313|EMBL:EJL21190.1};
OS   Novosphingobium sp. AP12.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1144305 {ECO:0000313|EMBL:EJL21190.1, ECO:0000313|Proteomes:UP000007515};
RN   [1] {ECO:0000313|EMBL:EJL21190.1, ECO:0000313|Proteomes:UP000007515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP12 {ECO:0000313|EMBL:EJL21190.1,
RC   ECO:0000313|Proteomes:UP000007515};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(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=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000256|PIRSR:PIRSR617512-2};
CC       Note=Binds 1 heme c group per subunit. {ECO:0000256|PIRSR:PIRSR617512-
CC       2};
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:EJL21190.1}.
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DR   EMBL; AKKE01000171; EJL21190.1; -; Genomic_DNA.
DR   RefSeq; WP_007687931.1; NZ_AKKE01000171.1.
DR   AlphaFoldDB; J2FVJ8; -.
DR   STRING; 1144305.PMI02_05261; -.
DR   PATRIC; fig|1144305.3.peg.4799; -.
DR   eggNOG; COG2010; Bacteria.
DR   eggNOG; COG4993; Bacteria.
DR   Proteomes; UP000007515; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
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   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   Pfam; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 5.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS51007; CYTC; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR617512-3};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR617512-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR617512-3};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007515};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..810
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003747706"
FT   DOMAIN          610..689
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         197..198
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         261
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         281
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         353
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         624
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         627
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         628
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         667
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
SQ   SEQUENCE   810 AA;  86842 MW;  3AA1B6122DF5F3F4 CRC64;
     MVAHYRKAAL RLALAALVPL SLGLAACNRP AQPIEEAMVA DPDEWPSWGR TGSEAHYSPL
     DEIDTGNVAN LKLAWHFDLE PGYSASTPLM AEGKVFLTSG HSHIRALDAV TGEQLWEYDG
     GTRERAKSAL QMSWGNKGIA YDAGHVFLVT TDGYVISLDA KTGKEAWKTY DYPDQSPRNS
     NGAPRVFGGK VIVGFGGADI SPARGFVTAY DAKTGKLAWR FYTTPGDPVT KANEKAEAVM
     RKTWPSGWMN PDGSRRGGGA TAWNAFSYDP ELRLVYLGLG NGFPYNQQKR SPGGGDNLFI
     ASIVAVNVDT GEYKWHYQVC PGEQWNCTAT TDMTLATLEI GGKERKVLMQ APKNGFFYVL
     DRATGEFISA EKIAKVTWAD HIDKKTGRPV ENPGIRYNGK PGLFEMWPGP TGAHSWMPQA
     YSPLTGLVYI PVLDNGALIG DGQKGGGEIT AGMGVTLLPE VELPGSHKSY LKAWNPVTQT
     EAWRVDLPGN WPGGVMASAG GLVFQGQVDG KFVARDAKTG KELWSFKTES PIVGAPITYR
     VNGRQYVTVI TGNGGNGAGI NSPGLAAFRT DYRLPRRVLT FALDGKDTIP PFEMPALTPP
     ADPDFKPDLA RAQAGAMLFG TRACLVCHGW NAVGGGAAPD LRYSPTITDA ATFKAIVKDG
     GLKMNGMPPF PAFTDEELET MRFYLRARAQ AAPAEAQALL DKAKAAKASN ARPQDFAGRW
     NITIQSPVGA QKAVMDLKVV GNVVTGKVVA EQGSVDVAGA VKDGRAKFQG KASMPMPITI
     SYDLTVRDGE LVGDNANGPF GTFPVTGVRP
//
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