CYC4_AZOVI
ID CYC4_AZOVI Reviewed; 210 AA.
AC P43302;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cytochrome c4;
DE Flags: Precursor;
GN Name=cycA;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CA;
RX PubMed=7619830; DOI=10.1016/0005-2728(95)00043-i;
RA Ng T.C.N., Laheri A.N., Maier R.J.;
RT "Cloning, sequencing, and mutagenesis of the cytochrome c4 gene from
RT Azotobacter vinelandii: characterization of the mutant strain and a
RT proposed new branch in the respiratory chain.";
RL Biochim. Biophys. Acta 1230:119-129(1995).
RN [2]
RP PROTEIN SEQUENCE OF 21-210.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=6089759; DOI=10.1042/bj2220217;
RA Ambler R.P., Daniel M., Melis K., Stout C.D.;
RT "The amino acid sequence of the dihaem cytochrome c4 from the bacterium
RT Azotobacter vinelandii.";
RL Biochem. J. 222:217-227(1984).
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; L37290; AAA87314.1; -; Genomic_DNA.
DR PIR; I39740; I39740.
DR RefSeq; WP_012698889.1; NZ_FPKM01000002.1.
DR AlphaFoldDB; P43302; -.
DR SMR; P43302; -.
DR OMA; AGCHSPN; -.
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 Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Periplasm; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:6089759"
FT CHAIN 21..210
FT /note="Cytochrome c4"
FT /id="PRO_0000006507"
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"
SQ SEQUENCE 210 AA; 21687 MW; 4B09C4AA90D1FC74 CRC64;
MNKALVTLLL TLGITGLAHA AGDAAAGQGK AAVCGACHGP DGNSAAPNFP KLAGQGERYL
LKQMQDIKAG TKPGAPEGSG RKVLEMTGML DNFSDQDLAD LAAYFTSQKP TVGAADPQLV
EAGETLYRGG KLADGMPACT GCHSPNGEGN TPAAYPRLSG QHAQYVAKQL TDFREGARTN
DGDNMIMRSI AAKLSNKDIA AISSYIQGLH