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Entry: E8V698_TERSS
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ID   E8V698_TERSS            Unreviewed;       742 AA.
AC   E8V698;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Quinoprotein glucose dehydrogenase {ECO:0000313|EMBL:ADV84989.1};
DE            EC=1.1.5.2 {ECO:0000313|EMBL:ADV84989.1};
GN   OrderedLocusNames=AciPR4_4246 {ECO:0000313|EMBL:ADV84989.1};
OS   Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Terriglobus.
OX   NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV84989.1, ECO:0000313|Proteomes:UP000006844};
RN   [1] {ECO:0000313|EMBL:ADV84989.1, ECO:0000313|Proteomes:UP000006844}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC   {ECO:0000313|Proteomes:UP000006844};
RX   PubMed=23450133; DOI=10.4056/sigs.3036810;
RA   Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA   Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT   "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT   an Acidobacteria from tundra soil.";
RL   Stand. Genomic Sci. 7:59-69(2012).
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; CP002467; ADV84989.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8V698; -.
DR   STRING; 401053.AciPR4_4246; -.
DR   KEGG; tsa:AciPR4_4246; -.
DR   eggNOG; COG4993; Bacteria.
DR   HOGENOM; CLU_018478_1_1_0; -.
DR   Proteomes; UP000006844; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0008876; F:quinoprotein glucose dehydrogenase activity; IEA:UniProtKB-EC.
DR   CDD; cd10280; PQQ_mGDH; 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; IPR017511; PQQ_mDH.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   PANTHER; PTHR32303:SF4; QUINOPROTEIN GLUCOSE DEHYDROGENASE; 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.
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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ADV84989.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006844};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          499..575
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  80140 MW;  DF8600B02FB31723 CRC64;
     MPHTRAASSR VYGYSRKART VSESSPQESS KTKQASHPHI AKSAIYGAPG VLALLTLFTT
     TLFAQQNQDW PIYNGRTTGD HYSPLTQINR TNVKTLKQAW TFDTGDQGIW ESSPLIVGRT
     LFIATPTGSI VALDGATGKQ QWRFDPETKS RQPIRGLAYL PEGKILAGIM SYLYELDAKT
     GKPVETFGKQ GRIDLREDLD TDPAKATVAL TSPGVVYKDL IILGFRAPET HPAPRGDIRA
     YDVHTGKLRW TFHTIPHPGE FGYDTWAAGA WEHAGAANAW AGMVVDQPRG IVYIPTGSAV
     DDFYGGDRIG NNLFANTLLA LDAATGKRLW HFQGIHHDIW DRDFPAPPVL LTVQHNGKPV
     DAVAQTTKQG YVYLFDRVTG TPLFPIEEMK VLPSTVPGEK SSPTQPHSLL PEPLARQTLT
     ADTLTTRSPE AHANALEQFK AMRSEGQFVP LSVDRITAVT PGMDGGAEWG GAAVDPRSGI
     LYVNANDIPY ITGLTANKPQ SSAGAAIYNS QCAMCHAADR KGSPPAFPSL VGITDRLTPA
     QITDTVQNGK GRMPGFPNVQ GEALQSLTDF LRAGKEDIVS GAAAEKTTER ELASTGNVPT
     PFRFLGYKRF VDQDGYPASA PPWGTLNAID MNTGKYLWRI PFGAYPELSA KGIPTTGTEN
     YGGPVLTASG LLFIASTIFD RQMHAYDTRT GELLWHTELP FGGLATPATY AINGKQYVVI
     ATGGGKDPTH PLGGTLVTFA LP
//
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