CYCL_METEA
ID CYCL_METEA Reviewed; 197 AA.
AC P14774; C5AQA7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cytochrome c-L;
DE Flags: Precursor;
GN Name=moxG; Synonyms=mxaG; OrderedLocusNames=MexAM1_META1p4536;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2842733; DOI=10.1093/nar/16.15.7722;
RA Nunn D.N., Anthony C.;
RT "The nucleotide sequence and deduced amino acid sequence of the genes for
RT cytochrome cL and a hypothetical second subunit of the methanol
RT dehydrogenase of Methylobacterium AM1.";
RL Nucleic Acids Res. 16:7722-7722(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2851998; DOI=10.1042/bj2560673;
RA Nunn D.N., Anthony C.;
RT "The nucleotide sequence and deduced amino acid sequence of the cytochrome
RT cL gene of Methylobacterium extorquens AM1, a novel class of c-type
RT cytochrome.";
RL Biochem. J. 256:673-676(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RX PubMed=2116368; DOI=10.1016/0378-1119(90)90457-3;
RA Anderson D.J., Morris C.J., Nunn D.N., Anthony C., Lidstrom M.E.;
RT "Nucleotide sequence of the Methylobacterium extorquens AM1 moxF and moxJ
RT genes involved in methanol oxidation.";
RL Gene 90:173-176(1990).
CC -!- FUNCTION: Electron acceptor for MDH. Acts in methanol oxidation.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is about +256 mV.;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; X07856; CAA30704.1; -; Genomic_DNA.
DR EMBL; CP001510; ACS42167.1; -; Genomic_DNA.
DR EMBL; M31108; AAA25382.1; -; Genomic_DNA.
DR RefSeq; WP_003599117.1; NC_012808.1.
DR PDB; 2C8S; X-ray; 1.60 A; A=26-197.
DR PDBsum; 2C8S; -.
DR AlphaFoldDB; P14774; -.
DR SMR; P14774; -.
DR STRING; 272630.MexAM1_META1p4536; -.
DR EnsemblBacteria; ACS42167; ACS42167; MexAM1_META1p4536.
DR KEGG; mea:Mex_1p4536; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_109361_0_0_5; -.
DR OMA; NGMMGPH; -.
DR OrthoDB; 1315115at2; -.
DR EvolutionaryTrace; P14774; -.
DR Proteomes; UP000009081; Chromosome.
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..25
FT CHAIN 26..197
FT /note="Cytochrome c-L"
FT /id="PRO_0000006552"
FT BINDING 90
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 93
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 94
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 STRAND 55..58
FT /evidence="ECO:0007829|PDB:2C8S"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:2C8S"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:2C8S"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:2C8S"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:2C8S"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2C8S"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:2C8S"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2C8S"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:2C8S"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2C8S"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:2C8S"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2C8S"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:2C8S"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2C8S"
SQ SEQUENCE 197 AA; 21226 MW; 58F22BACB90258CE CRC64;
MMNRVKIGTA LLGLTLAGIA LPALAQPQSG PQTGVVFRNT VTGEALDVSQ GKEGGRDTPA
VKKFLETGEN LYIDDKSCLR NGESLFATSC SGCHGHLAEG KLGPGLNDNY WTYPSNTTDV
GLFATIFGGA NGMMGPHNEN LTPDEMLQTI AWIRHLYTGP KQDAVWLNDE QKKAYTPYKQ
GEVIPKDAKG QCKPLDE
