ID A0A0C1L0F9_9BACT Unreviewed; 730 AA.
AC A0A0C1L0F9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Pyrrolo-quinoline quinone {ECO:0000313|EMBL:KIC93472.1};
GN ORFNames=OI18_17075 {ECO:0000313|EMBL:KIC93472.1};
OS Flavihumibacter solisilvae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1349421 {ECO:0000313|EMBL:KIC93472.1, ECO:0000313|Proteomes:UP000031408};
RN [1] {ECO:0000313|EMBL:KIC93472.1, ECO:0000313|Proteomes:UP000031408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-3 {ECO:0000313|EMBL:KIC93472.1,
RC ECO:0000313|Proteomes:UP000031408};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter solisilvae 3-3.";
RL Submitted (NOV-2014) 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:KIC93472.1}.
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DR EMBL; JSVC01000019; KIC93472.1; -; Genomic_DNA.
DR RefSeq; WP_039141975.1; NZ_JSVC01000019.1.
DR AlphaFoldDB; A0A0C1L0F9; -.
DR STRING; 1349421.OI18_17075; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000031408; 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; 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:UP000031408};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 488..563
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 730 AA; 80485 MW; 75F6DE5E95E9A1D4 CRC64;
MKKISFSAAV ISILLTAACE NGHHAATSDH SRGWEVYGGS NEGTRFSAFN QVDTSNVAQL
EVAWEYHTGD ADIENFSQIQ CNPIIVDAVM YGTSPQQKVF AIDASTGKEF WTFDPLSALE
SDEGRFVMNN TRGLSYWTDG KAKRIFFTAG PFLHSIDATT GRLDSAFGRF GKVDLHEGLG
RDVSGMFITN TSPGVVYKDL LILGSRVDEG PVAAPGHIRA YNVRSGKQEW IFHTIPQPGE
DGFESWEDPN AWKYIGGANC WSGFTLDEKR GIVFAPTGSA SYDFYGGMRK GANLFADCVL
ALDAATGKRR WHFQQIHHDL WDRDLPTPPA LVTVKHNGKD VDAVAQPTKT GYIFLLDRET
GEPLFPVNEL PVPVETDLAG EKVYPTQPVP VLPKPFVRQS ITENDINDLV SPEEQRELKQ
KLATLNHSHM FQAPSKKGTV IFPGYDGGAE WGGPAFDPST GIIYVNANEM PWILQMLDAK
NEQPKSENWL QAGKRLYGMH CQSCHGVDTK GGGHYPSLLN MEKRYSQPQF DSLLLSGRRM
MPSFQHLQEE ERKAIASYIL SLKADQEKRF TVPPSTPDTF RQLPYMGAGY TKFRTKDGQP
AIRPPWGTLT AIDLNSGQHV WQIPLGEIPE LKAKGHHTGT ENYGGPVVTS GGLVFIAATS
DRKMRAFNKR TGQLLWEFTL PASGFATPSV YEVSGRQYIV IACGGGKLRT KSGDSYVAFA
LPSTGEPGKK
//
