Cytochrome c'

Details

Name
Cytochrome c'
Kind
protein
Synonyms
Not Available
Gene Name
Not Available
UniProtKB Entry
P00138Swiss-Prot
Organism
Alcaligenes xylosoxydans xylosoxydans
NCBI Taxonomy ID
85698
Amino acid sequence
>lcl|BSEQ0012067|Cytochrome c'
QFAKPEDAVKYRQSALTLMASHFGRMTPVVKGQAPYDAAQIKANVEVLKTLSALPWAAFG
PGTEGGDARPEIWSDAASFKQKQQAFQDNIVKLSAAADAGDLDKLRAAFGDVGASCKACH
DAYRKKK
Number of residues
127
Molecular Weight
13628.35
Theoretical pI
9.52
GO Classification
Functions
electron carrier activity / heme binding / iron ion binding
Processes
electron transport chain
Components
periplasmic space
General Function
Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.
Specific Function
electron transfer activity
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
Not Available
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00138
UniProtKB Entry NameCYCP_ALCXX
PDB ID(s)1CGN, 1CGO, 1E83, 1E84, 1E85, 1E86, 2XL6, 2XL8, 2XLD, 2XLE, 2XLH, 2XLM, 2XLO, 2XLV, 2XLW, 2XM0, 2XM4, 2YKZ, 2YL0, 2YL1, 2YL3, 2YL7, 2YLD, 2YLG, 2YLI, 3ZQV, 3ZQY, 3ZTM, 3ZTZ, 3ZWI, 4CDA, 4CDV, 4CDY, 4CIP, 4CJG, 4CJO, 4D4N, 4D4X, 4WGY, 4WGZ, 5AGF
General References
  1. Ambler RP: The amino acid sequence of cytochrome c' from Alcaligenes sp. N.C.I.B. 11015. Biochem J. 1973 Dec;135(4):751-8. [Article]
  2. Dobbs AJ, Anderson BF, Faber HR, Baker EN: Three-dimensional structure of cytochrome c' from two Alcaligenes species and the implications for four-helix bundle structures. Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):356-68. [Article]
  3. Lawson DM, Stevenson CE, Andrew CR, Eady RR: Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase. EMBO J. 2000 Nov 1;19(21):5661-71. [Article]
  4. Andrew CR, Green EL, Lawson DM, Eady RR: Resonance Raman studies of cytochrome c' support the binding of NO and CO to opposite sides of the heme: implications for ligand discrimination in heme-based sensors. Biochemistry. 2001 Apr 3;40(13):4115-22. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Pidolic acidapproved, investigationalunknowntargetDetails