ID A0A1M7M0B5_9BACT Unreviewed; 703 AA.
AC A0A1M7M0B5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Quinoprotein glucose dehydrogenase {ECO:0000313|EMBL:SHM83561.1};
GN ORFNames=SAMN04488057_1045 {ECO:0000313|EMBL:SHM83561.1};
OS Cyclobacterium lianum.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=388280 {ECO:0000313|EMBL:SHM83561.1, ECO:0000313|Proteomes:UP000184513};
RN [1] {ECO:0000313|EMBL:SHM83561.1, ECO:0000313|Proteomes:UP000184513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6102 {ECO:0000313|EMBL:SHM83561.1,
RC ECO:0000313|Proteomes:UP000184513};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRCY01000004; SHM83561.1; -; Genomic_DNA.
DR RefSeq; WP_073093840.1; NZ_FRCY01000004.1.
DR AlphaFoldDB; A0A1M7M0B5; -.
DR STRING; 388280.SAMN04488057_1045; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000184513; 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; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 2.
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:UP000184513};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 471..548
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 703 AA; 77250 MW; A764AE9E84483F8B CRC64;
MENHPHFSTY RIITLCFLAL YGSACTQTTP EGAGADWATY LGHPTSNQYS TLDQINKDNV
SQLELTWTYK TGDSANYQTN NLIVDGWLYT ATPHSRVVAL DGATGKEYWT FDPSAVYESL
ADGDQRGLMY WHDGDIGHIL TMKGNRLFAL NAKTGEPIVS FGENGSIHLG EAMDIPGRPN
VTLNTPGQIY KDLFIIGANV GEDVPGAIRA FDIRTGKRKW IFHSLPRPGE FGSDTWPANY
LEKTGGASDW SGLALDEARG IVYVSTETAG PDFYGGDRYG ENLFANSLIA LDANTGQRLW
HHQLVHHDLW DMDIPQAPTL LTVEHEGKEL DIVAVGTKMG LLFVYDRVTG EPLWPIEERS
QAATKIDEIQ TWPTQPFPTA PPPLMRQEYT ADDFSTISPR AQQMSKEVFS QSGNYGAYPP
PSTGQTIMFP GYDGGMEWGG AAADPDGILY VNVNEIPWFY QLVPTKKADG SPLPNGEKQY
LIHCASCHGT DRKGNPDGGF PSLEGISGRW SKETVMQLMK KGGGRMPAFD QVAQGRLDAI
VRFLFNEEPA VSDETERKNQ APSYVFRGFQ RWNDEEGYPA IKPPWGTLNA VDLNTGTIKW
KVPLGEYEEL TKRGVPVTGT ENYGGPVVTA GGLLFIAATA DAKIRAFDKD NGKVLWEYQL
PAEGHATPSV YAVNGKQYLA ISVGGSKLKP HPEGAVFVFS LPD
//
