ID A0A0P7B8W9_9BACT Unreviewed; 743 AA.
AC A0A0P7B8W9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Quinoprotein glucose dehydrogenase {ECO:0000313|EMBL:KPM46757.1};
GN ORFNames=AFM12_18535 {ECO:0000313|EMBL:KPM46757.1};
OS Jiulongibacter sediminis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Jiulongibacter.
OX NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM46757.1, ECO:0000313|Proteomes:UP000050454};
RN [1] {ECO:0000313|EMBL:KPM46757.1, ECO:0000313|Proteomes:UP000050454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN14-9 {ECO:0000313|EMBL:KPM46757.1,
RC ECO:0000313|Proteomes:UP000050454};
RA Liu Y., Du J., Shao Z.;
RT "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL Submitted (JUL-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:KPM46757.1}.
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DR EMBL; LGTQ01000015; KPM46757.1; -; Genomic_DNA.
DR RefSeq; WP_055151633.1; NZ_LGTQ01000015.1.
DR AlphaFoldDB; A0A0P7B8W9; -.
DR STRING; 1605367.AFM12_18535; -.
DR PATRIC; fig|1605367.3.peg.1148; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000050454; Unassembled WGS sequence.
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 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; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR PANTHER; PTHR32303:SF10; OUTER MEMBRANE PROTEIN ASSEMBLY FACTOR BAMB; 1.
DR PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
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:UP000050454};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..743
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006135507"
FT DOMAIN 471..545
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 743 AA; 82807 MW; 578ACC3E50C6DECD CRC64;
MIKSKYHLVL VCGILFASIS CKKNQTNNTW THYGGSPEQS RYFEASEITK ENVAGLEVAW
VYETSDDVFN FFSPIVVDTI MYVYGKNSSL SAINAVTGKE IWIHSNLRGI TRRGINYWQS
KDGKDRRLIF TINNTLQSID AMTGKSILTF GNNGYVDLKE GLDRDPASIR RIQSMMPGVI
FEDLVILGSA PGENYFSPPG HVRAYNVVTG KMEWIFHTIP HPGEFGYDTW PKDAYKYAGG
ANVWSEISVD TERGIAYLPI GSPTFDFYGV DRLGSNLFGN SLVAVDARTG ERIWHYQTVH
HDLWDYDLSP APQLMTVNRK GKEVDAVAVA TKHGFLFVFD RVTGEPLFDI EEKPFPKSEM
EGEEAWPTQP IPTEIPSFTY HEVTPEILNP HFSEETRNYW IDRLSKAKTG LYVPPSSEYE
TVMMPGALGG ANYGNTAADP HKGIMYIMSQ TCASVYKLSK VEPPKIELST NDRTKAKTFY
DKTCQTCHGP NMEGSVGPTL KNVGDQYLYS EFKEIILNGR GQMPGFTHVD EETLNALYRL
LGGNPRRFNF GARSDEYVDP EGPVVASGGA PIEDDGKRAA PMADYPEGTE HPDVRYTSSY
DIEWTALVKP PWSYIMAYDL NTGKMLWKQP FGEDSLYTQG DPSVGAQNGT ARKGMIVTST
GIVFANGKGG KVYAFDSENG EILWQTTLSH ETNAQPSMYT VNGKQYLVIN AASSFTPDSY
DHSKKPGALP KGYVVYTLPN KKP
//