ID A0A1H4GB70_9SPHI Unreviewed; 723 AA.
AC A0A1H4GB70;
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:SEB06128.1};
GN ORFNames=SAMN05443550_109135 {ECO:0000313|EMBL:SEB06128.1};
OS Pedobacter hartonius.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=425514 {ECO:0000313|EMBL:SEB06128.1, ECO:0000313|Proteomes:UP000198850};
RN [1] {ECO:0000313|EMBL:SEB06128.1, ECO:0000313|Proteomes:UP000198850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19033 {ECO:0000313|EMBL:SEB06128.1,
RC ECO:0000313|Proteomes:UP000198850};
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; FNRA01000009; SEB06128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4GB70; -.
DR STRING; 425514.SAMN05443550_109135; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000198850; 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; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000198850};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 485..560
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 723 AA; 78998 MW; CDFA3BAF3E244CB2 CRC64;
MLIRKTKIIL TLIISAGVVA CAVYFLQNKD HGWKVYGGSS ENIKYSTLRQ IDTSNVSQLK
VAWVYHAEHD DTTRYGIMEC NPIIVDHTLY GVSPKMKLFA LDAATGKEKW HFDPADSLTN
KTWHRNSVNM NRGVSYWSDG DDRRIIYTVG PIAFAVNAGT GKLIGSFGKD GGIDLRKGLG
REEKDMSISP TSPAMIFKDL FIVSGAVNES TPGHIRAFDI RTGAQKWIFH TVPYPGEPGF
ETWDDPTAYK RMGSTNAWSG FTLDHKRGLL FAGIGSPTND FYGGDRSGKG LYGNAVIALD
AATGKLKWHF QAIHHDVWDM DISSPPALVS LKRNGKQVDA VVQTTKTGLI FVFERTTGKP
LFPVEERKVP VNGAVAGEHL SPSQPFPVLP KPFVRTIMTE KDLNHLGTDS SYQDIKQRFQ
TYRSEGIYTP PTEKGTIILP GYDGGANWGG PAIDPETGIL YINANEMAWV LNLVKDTSSA
KEGMTNHQAA ALLYSKNCMG CHGPERLGSG DYPSLIGVGK KYSLSEFSQL LSTGRRMMPG
FGHLSKDEKT ALASLVLDQK SEQDKRYKGS VIEKERSSKP SYTFTGYNKF LTKDGYPALS
PPWGTISAIN LNTGKYEWQV PFGEFEELKK KGIPTTGREN FGGPVVTAGG LLFIGASADG
YFRAIDKKTG KILWQTKLPA AAMATPAIYA IGGRQYVVIA CGGGKSGGKG GDSYVAFTLP
DQP
//
