ID F4C3K8_SPHS2 Unreviewed; 500 AA.
AC F4C3K8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Quinoprotein glucose dehydrogenase {ECO:0000313|EMBL:ADZ79396.1};
DE EC=1.1.5.2 {ECO:0000313|EMBL:ADZ79396.1};
GN OrderedLocusNames=Sph21_2849 {ECO:0000313|EMBL:ADZ79396.1};
OS Sphingobacterium sp. (strain 21).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ79396.1};
RN [1] {ECO:0000313|EMBL:ADZ79396.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21 {ECO:0000313|EMBL:ADZ79396.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT "Complete sequence of Sphingobacterium sp. 21.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002584; ADZ79396.1; -; Genomic_DNA.
DR AlphaFoldDB; F4C3K8; -.
DR STRING; 743722.Sph21_2849; -.
DR KEGG; shg:Sph21_2849; -.
DR PATRIC; fig|743722.3.peg.3042; -.
DR eggNOG; COG2010; Bacteria.
DR eggNOG; COG2133; Bacteria.
DR HOGENOM; CLU_012253_0_1_10; -.
DR OrthoDB; 9770043at2; -.
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:0008876; F:quinoprotein glucose dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1.
DR PANTHER; PTHR19328:SF13; HIPL1 PROTEIN; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF07995; GSDH; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 4: Predicted;
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:0000313|EMBL:ADZ79396.1}.
FT DOMAIN 404..481
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 500 AA; 55958 MW; C9B03E78874EDB21 CRC64;
MKKKCIAWLL IIYGIFLFFT CKHTDKQEEE APIFLLDSTY VRVNIVASHL DVPWEITSGP
DDEIWFTEQS GKVNKIDAKS GHIKTLLTLP NLYRERTAGL LGMVTHPNMS ETPYVFIAYS
ARKSDQVHVS RVVRYTYEAD TLVHPLTILE YPAWKGHFGA RVAIAPDGKL IIATGDGAQN
ENAQNLASPN GKILRFNIDG SIPSDNPFPN NAVWAWGLRN PQGLVFSPKG ILYNSDHGDA
TDDEVNIIQR GGNYGWPKIA GYVDSQEERL FAQDSILAPP LHAWTPTIAP AGLAYYASAE
IPEWKNTLLL ATLKGNSLYA LPLNKEGTKA DTVYHFFERT FGRIRAVYAS PDGTVYMATS
NRDWNPNGFA EENDDRILQI KKVDKSISTA NLVLKAKIAS NTKEMRSEGE ILYTNYCASC
HKPNGRGLTG TYPSLLHNKV VEGETAEFIR LILHGKNEMP SFSFLNDKDL AIVLSYVRKK
FASKGRQISK DDIKKERVNR
//
