ID A0A1K1PJ66_9BACT Unreviewed; 1131 AA.
AC A0A1K1PJ66;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glucose/arabinose dehydrogenase, beta-propeller fold {ECO:0000313|EMBL:SFW47840.1};
GN ORFNames=SAMN05661012_02044 {ECO:0000313|EMBL:SFW47840.1};
OS Chitinophaga sancti.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1004 {ECO:0000313|EMBL:SFW47840.1, ECO:0000313|Proteomes:UP000183788};
RN [1] {ECO:0000313|EMBL:SFW47840.1, ECO:0000313|Proteomes:UP000183788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 784 {ECO:0000313|EMBL:SFW47840.1,
RC ECO:0000313|Proteomes:UP000183788};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR602324-1}.
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DR EMBL; FPIZ01000005; SFW47840.1; -; Genomic_DNA.
DR RefSeq; WP_072359546.1; NZ_FPIZ01000005.1.
DR AlphaFoldDB; A0A1K1PJ66; -.
DR STRING; 1004.SAMN05661012_02044; -.
DR OrthoDB; 9816308at2; -.
DR Proteomes; UP000183788; 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:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002324; Cyt_c_ID.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR InterPro; IPR029010; ThuA-like.
DR PANTHER; PTHR40469:SF2; GALACTOSE-BINDING DOMAIN-LIKE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR40469; SECRETED GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR Pfam; PF07995; GSDH; 1.
DR Pfam; PF00801; PKD; 1.
DR Pfam; PF06283; ThuA; 1.
DR PRINTS; PR00606; CYTCHROMECID.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602324-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602324-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602324-1}.
FT DOMAIN 707..784
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 859..944
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 873
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
FT BINDING 877
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
FT BINDING 922
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
SQ SEQUENCE 1131 AA; 125034 MW; 6E30C89A69EE8DA0 CRC64;
MQLRYAIYLA ALCGIILSGC QSKTRPGNPR VLVFSKTAGF HHASIPAGIA AIEKLGKENG
FDVDTTTNAE MFVEDSLQKY AAVIFLNTTG DVLNNYQEAD FERYIQSGGG YVGVHAATDT
EYEWGWYGGL AGAYFDNHPA GTHKATLIVK DKSFGQLPDK WEHEDEWYNF KKISPNIKVI
MTVDEKTYEG GKNGEQHPIS WYHEYDGGRA FYTELGHTDA SYKEENFLKL LLSGIKYAVG
KNQLLDYNLA TTLRVPEEDR FTKNTLTSGE FFEPTEMTIL PDLNILIAQR RGEIMYFNQQ
AHKLTQAGFL RVYYKTEVPN VNAEEGVLGI SADPDFATNH YVYIYYSPVD TSVNRLSRFT
FENGKIDSAS EKIVLQLYSQ RNICCHTGGS IAFGADHLLY LSTGDNSTPF DEPGQQYVSK
GYGPLDDRPG HLNYDGRRTS ANTNDLRGKI LRIKINPDGT YTIPEGNLFK QGTAKTRPEI
YAMGTRNPYR ISVDRKNGYV YWGEVGPDAN NDDPERGPRG YDEINQAKKP GNFGYPMFVG
NNYAYHRYDY ETGKAGAPFD AAKPVNDSRN NTGIRDLPPA TPPMIWYPYD KSPDFPSMGS
GGRNAMAGPV YYNEFYPQET RFPDYYNGKF FIYDWVRGWI KAVTFDKDGN LSKTEPFMSH
TKFNAIIDME MGPDGRLYLL EYGNGWFSKN KDAGLSRIDF NGGNRAPIAK IQASKLSGGL
PFKVKLSAKG SADPDHDPLT YIWYLGNGNK KETKEPEAEV TYSMAGEYAV SVEVVDNKGT
STRSEGIALY AGNETPEVKI NLTGNKTFYF PGKQVAYDVQ VVDKEDAANI KPENMYIRAE
YMEGSDQAGI PQQGHQIITG VIAGKNLFES GDCKTCHKLD EKSIGPAFKL VAEKYKDDPN
AKDYLANKII SGGGGVWGET AMSAHPTLTQ GEAHQLAEYV MSQGAQNKVA PSMPQKGTVS
PTAGKPEKDN GVLYLIASYT DQGGPNIRPL TGTATATLRS PKLVAANYDQ SFGVTSFEAD
GMKFLIPTAN SWVTYNNLDL TGVTGVGIAY YTQESLQYGY NVQVFLDKDG GTKLGEVLIG
PGAKVKAPNI ATISFAPVAD GKLHDLYIRI TAASADEKTS FGISRFELLS K
//
