YHCC_ECOLI
ID YHCC_ECOLI Reviewed; 309 AA.
AC P0ADW6; P45476; Q2M901;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein YhcC {ECO:0000305};
GN Name=yhcC; OrderedLocusNames=b3211, JW3178;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7901196; DOI=10.1128/jb.175.22.7160-7169.1993;
RA Ernsting B.R., Denninger J.W., Blumenthal R.M., Matthews R.G.;
RT "Regulation of the gltBDF operon of Escherichia coli: how is a leucine-
RT insensitive operon regulated by the leucine-responsive regulatory
RT protein?";
RL J. Bacteriol. 175:7160-7169(1993).
RN [4]
RP FUNCTION, AND COFACTOR.
RX PubMed=25117543; DOI=10.1039/c4mt00156g;
RA Estellon J., Ollagnier de Choudens S., Smadja M., Fontecave M.,
RA Vandenbrouck Y.;
RT "An integrative computational model for large-scale identification of
RT metalloproteins in microbial genomes: a focus on iron-sulfur cluster
RT proteins.";
RL Metallomics 6:1913-1930(2014).
CC -!- FUNCTION: In vitro, can cleave S-adenosyl-L-methionine into methionine
CC and 5'-deoxyadenosine (AdoH). {ECO:0000269|PubMed:25117543}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:25117543};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000269|PubMed:25117543};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
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DR EMBL; U18997; AAA58013.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00096; AAC76243.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77255.1; -; Genomic_DNA.
DR EMBL; L20253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E65112; E65112.
DR RefSeq; NP_417678.1; NC_000913.3.
DR RefSeq; WP_001299745.1; NZ_SSZK01000007.1.
DR AlphaFoldDB; P0ADW6; -.
DR SMR; P0ADW6; -.
DR BioGRID; 4262426; 7.
DR BioGRID; 852046; 1.
DR DIP; DIP-48274N; -.
DR IntAct; P0ADW6; 10.
DR STRING; 511145.b3211; -.
DR PaxDb; P0ADW6; -.
DR PRIDE; P0ADW6; -.
DR EnsemblBacteria; AAC76243; AAC76243; b3211.
DR EnsemblBacteria; BAE77255; BAE77255; BAE77255.
DR GeneID; 947733; -.
DR KEGG; ecj:JW3178; -.
DR KEGG; eco:b3211; -.
DR PATRIC; fig|1411691.4.peg.3518; -.
DR EchoBASE; EB2660; -.
DR eggNOG; COG1242; Bacteria.
DR HOGENOM; CLU_060920_0_0_6; -.
DR InParanoid; P0ADW6; -.
DR OMA; NAGFTCP; -.
DR PhylomeDB; P0ADW6; -.
DR BioCyc; EcoCyc:G7669-MON; -.
DR PRO; PR:P0ADW6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR039661; ELP3.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR032432; Radical_SAM_C.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR005911; YhcC-like.
DR PANTHER; PTHR11135; PTHR11135; 1.
DR PANTHER; PTHR11135:SF1; PTHR11135:SF1; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF16199; Radical_SAM_C; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01091; uncharacterized_CHP01210-like; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR01212; TIGR01212; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..309
FT /note="Protein YhcC"
FT /id="PRO_0000169481"
FT DOMAIN 17..254
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 33
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9X0Z6"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9X0Z6"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9X0Z6"
FT CONFLICT 24..25
FT /note="KL -> NV (in Ref. 3; L20253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34607 MW; 61B3187BB77CA1A9 CRC64;
MQLQKLVNMF GGDLTRRYGQ KVHKLTLHGG FSCPNRDGTI GRGGCTFCNV ASFADEAQQH
RSIAEQLAHQ ANLVNRAKRY LAYFQAYTST FAEVQVLRSM YQQAVSQANI VGLCVGTRPD
CVPDAVLDLL CEYKDQGYEV WLELGLQTAH DKTLHRINRG HDFACYQRTT QLARQRGLKV
CSHLIVGLPG EGQAECLQTL ERVVETGVDG IKLHPLHIVK GSIMAKAWEA GRLNGIELED
YTLTAGEMIR HTPPEVIYHR ISASARRPTL LAPLWCENRW TGMVELDRYL NEHGVQGSAL
GRPWLPPTE
