CYCL_PARDE
ID CYCL_PARDE Reviewed; 177 AA.
AC P29899;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome c-L;
DE AltName: Full=Cytochrome c551I;
DE AltName: Full=Cytochrome c552;
DE Flags: Precursor;
GN Name=moxG;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Pd 1222;
RX PubMed=1657871; DOI=10.1128/jb.173.21.6948-6961.1991;
RA van Spanning R.J.M., Wansell C.W., de Boer T., Hazelaar M.J., Anazawa H.,
RA Harms N., Oltmann L.F., Stouthamer A.H.;
RT "Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of
RT Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the
RT resultant effect on methylotrophic growth.";
RL J. Bacteriol. 173:6948-6961(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8140419; DOI=10.1126/science.8140419;
RA Chen L., Durley R., Mathews F.S., Davidson V.L.;
RT "Structure of an electron transfer complex: methylamine dehydrogenase,
RT amicyanin, and cytochrome c551i.";
RL Science 264:86-90(1994).
CC -!- FUNCTION: Electron acceptor for MDH. Acts in methanol oxidation.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is about +190 mV.;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- INDUCTION: During growth on methanol.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; M57684; AAA25583.1; -; Genomic_DNA.
DR PIR; B41377; B41377.
DR RefSeq; WP_010399085.1; NZ_FOYK01000012.1.
DR PDB; 1MG2; X-ray; 2.25 A; D/H/L/P=23-177.
DR PDB; 1MG3; X-ray; 2.40 A; D/H/L/P=23-177.
DR PDB; 2GC4; X-ray; 1.90 A; D/H/L/P=23-169.
DR PDB; 2GC7; X-ray; 1.90 A; D/H/L/P=23-169.
DR PDB; 2MTA; X-ray; 2.40 A; C=23-169.
DR PDBsum; 1MG2; -.
DR PDBsum; 1MG3; -.
DR PDBsum; 2GC4; -.
DR PDBsum; 2GC7; -.
DR PDBsum; 2MTA; -.
DR AlphaFoldDB; P29899; -.
DR SMR; P29899; -.
DR DrugBank; DB08646; TRW3-(2-AMINO-3-HYDROXY-PROPYL)-6-(N'-CYCLOHEXYL-HYDRAZINO)OCTAHYDRO-INDOL-7-OL.
DR OMA; NGMMGPH; -.
DR EvolutionaryTrace; P29899; -.
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 GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR009153; Cyt_cL.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000008; Cytochrome_c551i; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR TIGRFAMs; TIGR03872; cytochrome_MoxG; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Metal-binding;
KW Methanol utilization; Periplasm; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..177
FT /note="Cytochrome c-L"
FT /id="PRO_0000006553"
FT BINDING 79
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 82
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
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 TURN 29..31
FT /evidence="ECO:0007829|PDB:2GC4"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2GC4"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2MTA"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2GC4"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:2GC4"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:2GC4"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2GC4"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:2GC4"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:2GC4"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2GC4"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2GC4"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:2GC4"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:2GC4"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:2GC4"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:2GC4"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2GC4"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:2GC4"
SQ SEQUENCE 177 AA; 19396 MW; 6949FBDC8B2C056E CRC64;
MTKPRILAAF AMTLIIPVAA MAAPQFFNII DGSPLNFDDA MEEGRDTEAV KHFLETGENV
YNEDPEILPE AEELYAGMCS GCHGHYAEGK IGPGLNDAYW TYPGNETDVG LFSTLYGGAT
GQMGPMWGSL TLDEMLRTMA WVRHLYTGDP KDASWLTDEQ KAGFTPFQPK SSGEDQS
