CYCP_ALCXX
ID CYCP_ALCXX Reviewed; 127 AA.
AC P00138;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cytochrome c';
OS Alcaligenes xylosoxydans xylosoxydans (Achromobacter xylosoxidans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=85698;
RN [1]
RP PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC STRAIN=LMG 1865 / CCUG 61957 / NCIMB 11015 / Iwasaki;
RX PubMed=4360249; DOI=10.1042/bj1350751;
RA Ambler R.P.;
RT "The amino acid sequence of cytochrome c' from Alcaligenes sp. N.C.I.B.
RT 11015.";
RL Biochem. J. 135:751-758(1973).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RC STRAIN=LMG 1865 / CCUG 61957 / NCIMB 11015 / Iwasaki;
RX PubMed=15299707; DOI=10.1107/s0907444995008328;
RA Dobbs A.J., Anderson B.F., Faber H.R., Baker E.N.;
RT "Three-dimensional structure of cytochrome c' from two Alcaligenes species
RT and the implications for four-helix bundle structures.";
RL Acta Crystallogr. D 52:356-368(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
RC STRAIN=LMG 1865 / CCUG 61957 / NCIMB 11015 / Iwasaki;
RX PubMed=11060017; DOI=10.1093/emboj/19.21.5661;
RA Lawson D.M., Stevenson C.E.M., Andrew C.R., Eady R.R.;
RT "Unprecedented proximal binding of nitric oxide to heme: implications for
RT guanylate cyclase.";
RL EMBO J. 19:5661-5671(2000).
RN [4]
RP RESONANCE RAMAN SPECTROSCOPY.
RC STRAIN=LMG 1865 / CCUG 61957 / NCIMB 11015 / Iwasaki;
RX PubMed=11300792; DOI=10.1021/bi0023652;
RA Andrew C.R., Green E.L., Lawson D.M., Eady R.R.;
RT "Resonance Raman studies of cytochrome c' support the binding of NO and CO
RT to opposite sides of the heme: implications for ligand discrimination in
RT heme-based sensors.";
RL Biochemistry 40:4115-4122(2001).
CC -!- FUNCTION: Cytochrome c' is the most widely occurring bacterial c-type
CC cytochrome. Cytochromes c' are high-spin proteins and the heme has no
CC sixth ligand. Their exact function is not known.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 1 heme group per subunit.
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DR PIR; A00131; CCALC.
DR PDB; 1CGN; X-ray; 2.15 A; A=2-127.
DR PDB; 1CGO; X-ray; 1.80 A; A=2-127.
DR PDB; 1E83; X-ray; 2.05 A; A=1-127.
DR PDB; 1E84; X-ray; 1.90 A; A=1-127.
DR PDB; 1E85; X-ray; 1.35 A; A=2-127.
DR PDB; 1E86; X-ray; 1.95 A; A=1-127.
DR PDB; 2XL6; X-ray; 1.07 A; A=2-127.
DR PDB; 2XL8; X-ray; 1.14 A; A=2-127.
DR PDB; 2XLD; X-ray; 1.40 A; A=2-127.
DR PDB; 2XLE; X-ray; 1.12 A; A=2-127.
DR PDB; 2XLH; X-ray; 1.14 A; A=2-127.
DR PDB; 2XLM; X-ray; 1.19 A; A=2-127.
DR PDB; 2XLO; X-ray; 1.24 A; A=2-127.
DR PDB; 2XLV; X-ray; 1.24 A; A=2-127.
DR PDB; 2XLW; X-ray; 1.17 A; A=2-123.
DR PDB; 2XM0; X-ray; 1.25 A; A=2-127.
DR PDB; 2XM4; X-ray; 1.10 A; A=2-127.
DR PDB; 2YKZ; X-ray; 0.84 A; A=2-127.
DR PDB; 2YL0; X-ray; 0.95 A; A=2-127.
DR PDB; 2YL1; X-ray; 1.03 A; A=2-127.
DR PDB; 2YL3; X-ray; 1.04 A; A=2-127.
DR PDB; 2YL7; X-ray; 0.90 A; A=2-127.
DR PDB; 2YLD; X-ray; 1.25 A; A=2-127.
DR PDB; 2YLG; X-ray; 1.05 A; A=2-127.
DR PDB; 2YLI; X-ray; 1.45 A; A=2-127.
DR PDB; 3ZQV; X-ray; 0.84 A; A=2-127.
DR PDB; 3ZQY; X-ray; 1.03 A; A=2-127.
DR PDB; 3ZTM; X-ray; 0.90 A; A=2-127.
DR PDB; 3ZTZ; X-ray; 1.05 A; A=2-127.
DR PDB; 3ZWI; X-ray; 1.25 A; A=2-127.
DR PDB; 4CDA; X-ray; 1.30 A; A=2-127.
DR PDB; 4CDV; X-ray; 1.17 A; A=2-127.
DR PDB; 4CDY; X-ray; 1.77 A; A=2-127.
DR PDB; 4CIP; X-ray; 1.22 A; A=2-127.
DR PDB; 4CJG; X-ray; 1.26 A; A=2-127.
DR PDB; 4CJO; X-ray; 1.55 A; A=2-127.
DR PDB; 4D4N; X-ray; 1.45 A; A=2-127.
DR PDB; 4D4X; X-ray; 1.30 A; A=2-127.
DR PDB; 4WGY; X-ray; 1.48 A; A=2-127.
DR PDB; 4WGZ; X-ray; 1.11 A; A=2-127.
DR PDB; 5AGF; X-ray; 1.09 A; A=2-127.
DR PDB; 5JLI; X-ray; 1.55 A; A=2-127.
DR PDB; 5JP7; X-ray; 1.26 A; A=2-126.
DR PDB; 5JRA; X-ray; 1.38 A; A=2-126.
DR PDB; 5JS5; X-ray; 1.70 A; A=2-125.
DR PDB; 5JSL; X-ray; 1.25 A; A=2-126.
DR PDB; 5JT4; X-ray; 1.25 A; A=2-125.
DR PDB; 5JUA; X-ray; 1.13 A; A=1-126.
DR PDB; 5JVE; X-ray; 1.12 A; A=2-125.
DR PDB; 5NC0; X-ray; 0.91 A; A=1-127.
DR PDB; 5NGX; X-ray; 1.06 A; A=1-126.
DR PDBsum; 1CGN; -.
DR PDBsum; 1CGO; -.
DR PDBsum; 1E83; -.
DR PDBsum; 1E84; -.
DR PDBsum; 1E85; -.
DR PDBsum; 1E86; -.
DR PDBsum; 2XL6; -.
DR PDBsum; 2XL8; -.
DR PDBsum; 2XLD; -.
DR PDBsum; 2XLE; -.
DR PDBsum; 2XLH; -.
DR PDBsum; 2XLM; -.
DR PDBsum; 2XLO; -.
DR PDBsum; 2XLV; -.
DR PDBsum; 2XLW; -.
DR PDBsum; 2XM0; -.
DR PDBsum; 2XM4; -.
DR PDBsum; 2YKZ; -.
DR PDBsum; 2YL0; -.
DR PDBsum; 2YL1; -.
DR PDBsum; 2YL3; -.
DR PDBsum; 2YL7; -.
DR PDBsum; 2YLD; -.
DR PDBsum; 2YLG; -.
DR PDBsum; 2YLI; -.
DR PDBsum; 3ZQV; -.
DR PDBsum; 3ZQY; -.
DR PDBsum; 3ZTM; -.
DR PDBsum; 3ZTZ; -.
DR PDBsum; 3ZWI; -.
DR PDBsum; 4CDA; -.
DR PDBsum; 4CDV; -.
DR PDBsum; 4CDY; -.
DR PDBsum; 4CIP; -.
DR PDBsum; 4CJG; -.
DR PDBsum; 4CJO; -.
DR PDBsum; 4D4N; -.
DR PDBsum; 4D4X; -.
DR PDBsum; 4WGY; -.
DR PDBsum; 4WGZ; -.
DR PDBsum; 5AGF; -.
DR PDBsum; 5JLI; -.
DR PDBsum; 5JP7; -.
DR PDBsum; 5JRA; -.
DR PDBsum; 5JS5; -.
DR PDBsum; 5JSL; -.
DR PDBsum; 5JT4; -.
DR PDBsum; 5JUA; -.
DR PDBsum; 5JVE; -.
DR PDBsum; 5NC0; -.
DR PDBsum; 5NGX; -.
DR AlphaFoldDB; P00138; -.
DR SASBDB; P00138; -.
DR SMR; P00138; -.
DR STRING; 1216976.AX27061_1806; -.
DR DrugBank; DB03088; Pidolic acid.
DR eggNOG; COG3909; Bacteria.
DR EvolutionaryTrace; P00138; -.
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 InterPro; IPR010980; Cyt_c/b562.
DR InterPro; IPR002321; Cyt_c_II.
DR InterPro; IPR012127; Cyt_c_prime.
DR InterPro; IPR015984; Cyt_c_prime_subgr.
DR Pfam; PF01322; Cytochrom_C_2; 1.
DR PIRSF; PIRSF000027; Cytc_c_prime; 1.
DR PRINTS; PR00608; CYTCHROMECII.
DR SUPFAM; SSF47175; SSF47175; 1.
DR PROSITE; PS51009; CYTCII; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Periplasm; Pyrrolidone carboxylic acid; Transport.
FT CHAIN 1..127
FT /note="Cytochrome c'"
FT /id="PRO_0000108369"
FT BINDING 116
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT BINDING 119
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT BINDING 120
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:4360249"
FT HELIX 5..24
FT /evidence="ECO:0007829|PDB:2YKZ"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:2YKZ"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:2YKZ"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2YKZ"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2XL6"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:2YKZ"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:2YKZ"
FT HELIX 102..123
FT /evidence="ECO:0007829|PDB:2YKZ"
SQ SEQUENCE 127 AA; 13628 MW; 6F6C7D6DF122640F CRC64;
QFAKPEDAVK YRQSALTLMA SHFGRMTPVV KGQAPYDAAQ IKANVEVLKT LSALPWAAFG
PGTEGGDARP EIWSDAASFK QKQQAFQDNI VKLSAAADAG DLDKLRAAFG DVGASCKACH
DAYRKKK
