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Database: UniProt
Entry: A0A1I3LYK1_9SPHI
LinkDB: A0A1I3LYK1_9SPHI
Original site: A0A1I3LYK1_9SPHI 
ID   A0A1I3LYK1_9SPHI        Unreviewed;       757 AA.
AC   A0A1I3LYK1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Quinoprotein glucose dehydrogenase {ECO:0000313|EMBL:SFI89792.1};
GN   ORFNames=SAMN05444682_106186 {ECO:0000313|EMBL:SFI89792.1};
OS   Parapedobacter indicus.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Parapedobacter.
OX   NCBI_TaxID=1477437 {ECO:0000313|EMBL:SFI89792.1, ECO:0000313|Proteomes:UP000198670};
RN   [1] {ECO:0000313|EMBL:SFI89792.1, ECO:0000313|Proteomes:UP000198670}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK1 {ECO:0000313|EMBL:SFI89792.1,
RC   ECO:0000313|Proteomes:UP000198670};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000256|ARBA:ARBA00001931};
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008156}.
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DR   EMBL; FOQO01000006; SFI89792.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3LYK1; -.
DR   STRING; 1477437.SAMN05444682_106186; -.
DR   OrthoDB; 7012117at2; -.
DR   Proteomes; UP000198670; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   PANTHER; PTHR32303:SF10; OUTER MEMBRANE PROTEIN ASSEMBLY FACTOR BAMB; 1.
DR   PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   Pfam; PF01011; PQQ; 3.
DR   SMART; SM00564; PQQ; 6.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198670};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          482..558
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          558..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  82427 MW;  6A959FA08F423F62 CRC64;
     MQRTAILGTL FLAVCWACHP DHATRYKAWS DYGGGPDHSK YVDYKQITRE NVNQLEIAFV
     YPTGDNVNYR FNPVIVDGVM YVLAKNNSLV AIDAATGKEL WIHANLRGII QRGVNFWQRK
     DRKEKRLLIC LNNTLQAIDA NTGKSITTFG KGGYVDLKQG LDRDPATFGR ATSTTPGKVF
     EDLIILGSAP GENLFSGPGH LRAYNVITGE LVWVFHTIPH PGEYGYDTWP AEAYKYVGGT
     NTWGEISVDE DRGIAYFPIG SPTYDYDGSD RAGSNLFGNC ILALDARTGK RLWHFQTVHH
     DIWDYDLTAA PQLITVNHGG KKIDAVAVAS KHGFLFVFDR VTGKPLWPIE ERPVPASDMP
     NETAWPTQPF PTVVPPFNRQ LVTVDDINPY FPPADKAKWT ARVAAAKNGL FHPLSDQYEV
     VTNPGAVGGA NFGNTAADPK NGIVYVQTQE LVDFYSLKKR ESAPQRGGPG FGGGRNSGVS
     PERLAQGKAL YMQHCQACHG ENRAGIDGLG ATLINLSTKV NAEAFKGIMA VGKGRMPGFP
     HLTETEIAAI YAYVTPEAQR GPGGRGNRDD DRVELPDGPV VASGGVPVDL PPSGGQRMTD
     YPSAYTGPRS EYVETNNWGL GVPNLLTPPW SLIVAYDLNE GKIKWKIPLG NDDSIPGSNN
     LSMPNGSQGK GMVVTSTGLL FSTCLDGRVY AYNTDDGSML WSAELGRSNP GGLPAMYEVD
     GRQYLVVCSV GSLKDKSKAE SDVPKGYIVY ALPKKEK
//
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