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CYC4_PSEST
ID   CYC4_PSEST              Reviewed;         210 AA.
AC   Q52369;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Cytochrome c4;
DE   Flags: Precursor;
GN   Name=cc4;
OS   Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11607 / DSM 50227 / LMG 1228 / NCIMB 9721 / NCTC 10475;
RX   PubMed=8026750; DOI=10.1016/0378-1119(94)90219-4;
RA   Christensen H.E.M.;
RT   "Cloning and characterisation of the gene encoding cytochrome c4 from
RT   Pseudomonas stutzeri.";
RL   Gene 144:139-140(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RC   STRAIN=ATCC 11607 / DSM 50227 / LMG 1228 / NCIMB 9721 / NCTC 10475;
RX   PubMed=9032080; DOI=10.1016/s0969-2126(97)00179-2;
RA   Kadziola A., Larsen S.;
RT   "Crystal structure of the dihaem cytochrome c4 from Pseudomonas stutzeri
RT   determined at 2.2-A resolution.";
RL   Structure 5:203-216(1997).
CC   -!- FUNCTION: Diheme, high potential cytochrome c believed to be an
CC       intermediate electron donor to terminal oxidation systems.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- PTM: Binds 2 heme c groups covalently per subunit.
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DR   EMBL; U05988; AAA20247.1; -; Genomic_DNA.
DR   RefSeq; WP_014818660.1; NZ_PJJZ01000003.1.
DR   PDB; 1ETP; X-ray; 2.20 A; A/B=21-210.
DR   PDB; 1M6Z; X-ray; 1.35 A; A/B/C/D=21-210.
DR   PDB; 1M70; X-ray; 1.25 A; A/B/C/D=21-210.
DR   PDBsum; 1ETP; -.
DR   PDBsum; 1M6Z; -.
DR   PDBsum; 1M70; -.
DR   AlphaFoldDB; Q52369; -.
DR   SMR; Q52369; -.
DR   STRING; 32042.PstZobell_09982; -.
DR   DrugBank; DB03317; Ferroheme C.
DR   EvolutionaryTrace; Q52369; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   Gene3D; 1.10.760.10; -; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR024167; Cytochrome_c4-like.
DR   Pfam; PF00034; Cytochrom_C; 2.
DR   PIRSF; PIRSF000005; Cytochrome_c4; 1.
DR   SUPFAM; SSF46626; SSF46626; 2.
DR   PROSITE; PS51007; CYTC; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW   Signal; Transport.
FT   SIGNAL          1..20
FT   CHAIN           21..210
FT                   /note="Cytochrome c4"
FT                   /id="PRO_0000006509"
FT   BINDING         34
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT   BINDING         37
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT   BINDING         38
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         86
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         139
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT   BINDING         142
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT   BINDING         143
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         187
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   HELIX           24..28
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           32..34
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           35..38
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           57..71
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   TURN            87..92
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           95..107
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           117..129
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           140..143
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           163..174
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   TURN            180..184
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           186..191
FT                   /evidence="ECO:0007829|PDB:1M70"
FT   HELIX           196..207
FT                   /evidence="ECO:0007829|PDB:1M70"
SQ   SEQUENCE   210 AA;  21742 MW;  C33CF23A6FAA6F99 CRC64;
     MNKVLVSLLL TLGITGMAHA AGDAEAGQGK VAVCGACHGV DGNSPAPNFP KLAGQGERYL
     LKQLQDIKAG STPGAPEGVG RKVLEMTGML DPLSDQDLED IAAYFSSQKG SVGYADPALA
     KQGEKLFRGG KLDQGMPACT GCHAPNGVGN DLAGFPKLGG QHAAYTAKQL TDFREGNRTN
     DGDTMIMRGV AAKLSNKDIE ALSSYIQGLH
 
 
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