ID A0A1I7AFZ3_9BACT Unreviewed; 705 AA.
AC A0A1I7AFZ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Quinoprotein glucose dehydrogenase {ECO:0000313|EMBL:SFT73790.1};
GN ORFNames=SAMN04489724_1934 {ECO:0000313|EMBL:SFT73790.1};
OS Algoriphagus locisalis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=305507 {ECO:0000313|EMBL:SFT73790.1, ECO:0000313|Proteomes:UP000199673};
RN [1] {ECO:0000313|EMBL:SFT73790.1, ECO:0000313|Proteomes:UP000199673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23445 {ECO:0000313|EMBL:SFT73790.1,
RC ECO:0000313|Proteomes:UP000199673};
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; FPBF01000002; SFT73790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7AFZ3; -.
DR STRING; 305507.SAMN04489724_1934; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000199673; Unassembled WGS sequence.
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:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR CDD; cd10280; PQQ_mGDH; 1.
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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 471..547
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 705 AA; 77566 MW; 14439F9D59063FBA CRC64;
MKPLLKVVFG SLLLFSACQP KTAKIDYTDW SHYGGPADGS RYSALTQITK NNVSQLEVAW
TYNTGDATAS SQIQCQPIVV NGLLYGSTPK LNVFALNAST GEEVWRFDPF EVLGGENSWA
GTNRGVSYWE DGDDKRILFG AGNWLMAVDA ETGEPILSFG DEGKVDLRKG LDTEREDFMI
VANAPGVVYG DLLIIGMRLS EGLDAAPGHI RAYNIRTGKR EWIFHTIPQE GEPGYETWDP
ATIKQIGGAN NWAGMTVDQE RGIVFVPTGS ATYDFWGGYR KGDNLYANTL IALNAQTGER
IWHFQAVHHD VWDRDFPANP NLIRIQKDGE WIDVVAQISK QGMTYVFDRA TGEPVWPIVE
TEVTQSVMPG EFTSATQPIP TLPEPFMNMV FDESSILSLK PEWEADIRNQ LEDAIYGDTW
APPHPEKPIV LFPGMDGGGE WGGASFDPET QTFYVNANQI PWIIGMTPNA DFENVGKSVY
TNYCGNCHGL DRKGNPPTIP SLLDLKEKFT YDSLDLLLRK GRGAMPAFDH ISTENRKVIL
EYLMDKALEV GDKQEIEGGK TQLFPRYYMD GYKKLVTKEG VYGSNPPWGL LTAIDMSTGK
KKWQVPLGEI DSLSGQGFAP TGTENYGGPV VTAGGILFIA ATKDEMIRAF DKETGEILWE
AKLPASGHAT PAVYEMNGKQ FLVIACGGGK GTKSGDAYVA FALPD
//
