ID A0A0Q5T0F4_9BACT Unreviewed; 709 AA.
AC A0A0Q5T0F4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Pyrrolo-quinoline quinone {ECO:0000313|EMBL:KQS26833.1};
GN ORFNames=ASG33_20020 {ECO:0000313|EMBL:KQS26833.1};
OS Dyadobacter sp. Leaf189.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS26833.1, ECO:0000313|Proteomes:UP000051810};
RN [1] {ECO:0000313|EMBL:KQS26833.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS26833.1,
RC ECO:0000313|Proteomes:UP000051810};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS26833.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS26833.1,
RC ECO:0000313|Proteomes:UP000051810};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQS26833.1}.
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DR EMBL; LMPS01000006; KQS26833.1; -; Genomic_DNA.
DR RefSeq; WP_056289584.1; NZ_LMPS01000006.1.
DR AlphaFoldDB; A0A0Q5T0F4; -.
DR STRING; 1736295.ASG33_20020; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000051810; 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; 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:UP000051810};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 476..553
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 709 AA; 77188 MW; 6AB76FD1A1B2E8E9 CRC64;
MIKSITKKFL WVAVLSLSVF ISSRSLFIES PGEEKEWPEY LGGPDRNHYS SLTQINPGNV
NQLQVAWTYS MPDSGQTQVN PIVVDGVLYG VTSTVQAFAL DAFTGKQLWI FGDKSKNGSN
TSRGLTYWSD GDDKRILHAM GEFLYALDAK TGKPIQTFGE NGRIDLHTGL PEIAAKKYMV
SNTPGTIFED LIIMPLRLSE ESDAAPGDLR AFNVRTGKLV WTFHTIPYPG EFGYETFPPD
AYKNTYTGAA NNWAGTAIDR TRGILYVPTG SAGYDFYGGK RKGANLFSNC LLALDARTGK
RIWHFQTMHH DMWDRDLPAP PNLVTITKNG QKIDAVAQVS KQGYVFLFDR VTGKPIYPIR
EVTAPQAALP GEHPWPTQPV PTRPAAFARQ AYTLTENDIS PYAPDRDSLK AKFKTYKKAL
FAAPSKEGTV ILPGFDGGAE WGGAAADPEK GILYVNSNEM AWILTMKDTP KESELSALSP
GEKTYTTYCA TCHGAQRKGN AKSGYPSLVD IGSRRDRAFV SQLVTSGKGM MPGFPMLTAG
EKQALISFLF GDEKVEAVSQ TPASKKTFLP YQSTGYNKFL DANGLPAIAP PWGTLNAIDL
NTGKYLWKVP FGEVAALKAK GVPTTGTENY GGPVVTASGL LFIAATKDGK FRVFDKANGK
LLWETMLPAA GFATPATYEA NGKQFVVIAC GGTKLGTKKG NQYVAFALP
//
