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Database: UniProt
Entry: A0A3N4MMY0_9BACT
LinkDB: A0A3N4MMY0_9BACT
Original site: A0A3N4MMY0_9BACT 
ID   A0A3N4MMY0_9BACT        Unreviewed;       504 AA.
AC   A0A3N4MMY0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Quinoprotein glucose dehydrogenase {ECO:0000313|EMBL:RPD41400.1};
GN   ORFNames=EG028_08765 {ECO:0000313|EMBL:RPD41400.1};
OS   Chitinophaga barathri.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1647451 {ECO:0000313|EMBL:RPD41400.1, ECO:0000313|Proteomes:UP000279089};
RN   [1] {ECO:0000313|Proteomes:UP000279089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLT18 {ECO:0000313|Proteomes:UP000279089};
RA   Zong Y.;
RT   "Chitinophaga lutea sp.nov., isolate from arsenic contaminated soil.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RPD41400.1}.
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DR   EMBL; RMBX01000004; RPD41400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4MMY0; -.
DR   OrthoDB; 9770043at2; -.
DR   Proteomes; UP000279089; 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; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR012938; Glc/Sorbosone_DH.
DR   InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR   PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR19328:SF13; HIPL1 PROTEIN; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   Pfam; PF07995; GSDH; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR   PROSITE; PS51007; CYTC; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
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}; Reference proteome {ECO:0000313|Proteomes:UP000279089};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..504
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018101356"
FT   DOMAIN          401..483
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   504 AA;  55254 MW;  4A11F41A140593EB CRC64;
     MKTSWPILLL LLCLTAGSAC RQGTHTSFSQ PPESALVLDS TTLGVSTVIQ DLNVPWEIYW
     GPDDRIWFTE QSGTISAVMP ETGERKVMLV IPEVYRQRSL GLLGMALHPT EPYVFVDYTH
     LKKNSTIVSK LVRYTRTKDT LKDPLLLLEF PGNTGHNGSR VTIAPDGKVM LATGDAARYP
     NAPDTASLNG KILRMNTDGS VPADNPYPGK LLWSRGHRNI QGLAFTSNGH FFASEHGDAT
     DDELNLIRQT GYYAWPHIEG YADRPKEKAY ADTFAFIPPV FSWTPTIAPA GIDHYLSGKI
     PEWRNSLLMV TLKNASLRVI RLNETQDSVL GETVYLSGIF GRLRDLCVSP SGDIYLATSN
     RDWNPGKGFP KEHDDKIIRL SPIPSAGNLP VLPQSANLNT ASLAKGAMLY ASYCEACHKP
     DGRGIKGSFP KLDKSPVVTG DAAALLQLIL KGSKKNTGEQ MPGFAFMPDE DIASVVSYIR
     GAWYNQADSV SATDVQKERK KAGQ
//
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