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CYC6_NOSS1
ID   CYC6_NOSS1              Reviewed;         111 AA.
AC   P0A3X7; P28596;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cytochrome c6;
DE   AltName: Full=Cytochrome c-553;
DE   AltName: Full=Cytochrome c553;
DE   AltName: Full=Soluble cytochrome f;
DE   Flags: Precursor;
GN   Name=petJ; Synonyms=cytA; OrderedLocusNames=alr4251;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8025680; DOI=10.1099/13500872-140-5-1151;
RA   Ghassemian M., Wong B., Ferreira F., Markley J.L., Straus N.A.;
RT   "Cloning, sequencing and transcriptional studies of the genes for
RT   cytochrome c-553 and plastocyanin from Anabaena sp. PCC 7120.";
RL   Microbiology 140:1151-1159(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- FUNCTION: Functions as an electron carrier between membrane-bound
CC       cytochrome b6-f and photosystem I in oxygenic photosynthesis.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid lumen {ECO:0000305}.
CC   -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M97009; AAA59365.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB75950.1; -; Genomic_DNA.
DR   PIR; AD2337; AD2337.
DR   PIR; I39601; I39601.
DR   RefSeq; WP_010998389.1; NZ_RSCN01000010.1.
DR   PDB; 4GYD; X-ray; 1.80 A; A/B/C/D/E/F=26-111.
DR   PDB; 4H0J; X-ray; 2.00 A; A/B/C/D/E/F=26-111.
DR   PDB; 4H0K; X-ray; 1.95 A; A/B=26-111.
DR   PDBsum; 4GYD; -.
DR   PDBsum; 4H0J; -.
DR   PDBsum; 4H0K; -.
DR   AlphaFoldDB; P0A3X7; -.
DR   SMR; P0A3X7; -.
DR   MINT; P0A3X7; -.
DR   STRING; 103690.17133386; -.
DR   TCDB; 3.D.3.5.6; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR   EnsemblBacteria; BAB75950; BAB75950; BAB75950.
DR   KEGG; ana:alr4251; -.
DR   eggNOG; COG2010; Bacteria.
DR   OMA; GQNVIMP; -.
DR   OrthoDB; 1939800at2; -.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0031979; C:plasma membrane-derived thylakoid lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.760.10; -; 1.
DR   HAMAP; MF_00594; Cytc_PetJ; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR023655; Cyt_C6.
DR   InterPro; IPR008168; Cyt_C_IC.
DR   PANTHER; PTHR34688; PTHR34688; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PRINTS; PR00605; CYTCHROMECIC.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Electron transport; Heme; Iron; Metal-binding;
KW   Photosynthesis; Reference proteome; Signal; Thylakoid; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..111
FT                   /note="Cytochrome c6"
FT                   /id="PRO_0000023855"
FT   BINDING         39
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   HELIX           28..38
FT                   /evidence="ECO:0007829|PDB:4GYD"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:4GYD"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:4GYD"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:4GYD"
FT   HELIX           58..63
FT                   /evidence="ECO:0007829|PDB:4GYD"
FT   HELIX           69..78
FT                   /evidence="ECO:0007829|PDB:4GYD"
FT   TURN            87..89
FT                   /evidence="ECO:0007829|PDB:4H0K"
FT   HELIX           92..108
FT                   /evidence="ECO:0007829|PDB:4GYD"
SQ   SEQUENCE   111 AA;  11799 MW;  A82778FBFE87AE80 CRC64;
     MKKIFSLVLL GIALFTFAFS SPALAADSVN GAKIFSANCA SCHAGGKNLV QAQKTLKKAD
     LEKYGMYSAE AIIAQVTNGK NAMPAFKGRL KPEQIEDVAA YVLGKADADW K
 
 
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