TDCE_ECOLI
ID TDCE_ECOLI Reviewed; 764 AA.
AC P42632; Q2M994; Q6BF44;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=PFL-like enzyme TdcE;
DE AltName: Full=Keto-acid formate acetyltransferase;
DE AltName: Full=Keto-acid formate-lyase;
DE AltName: Full=Ketobutyrate formate-lyase;
DE Short=KFL;
DE EC=2.3.1.- {ECO:0000269|PubMed:9484901};
DE AltName: Full=Pyruvate formate-lyase;
DE Short=PFL;
DE EC=2.3.1.54 {ECO:0000269|PubMed:9484901};
GN Name=tdcE; Synonyms=yhaS; OrderedLocusNames=b3114, JW5522;
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 SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [3]
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 [4]
RP FUNCTION AS A LYASE AND IN THE THREONINE CATABOLISM, CATALYTIC ACTIVITY,
RP DISRUPTION PHENOTYPE, INDUCTION, ACTIVITY REGULATION, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=9484901; DOI=10.1046/j.1365-2958.1998.00696.x;
RA Hesslinger C., Fairhurst S.A., Sawers G.;
RT "Novel keto acid formate-lyase and propionate kinase enzymes are components
RT of an anaerobic pathway in Escherichia coli that degrades L-threonine to
RT propionate.";
RL Mol. Microbiol. 27:477-492(1998).
CC -!- FUNCTION: Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and
CC formate. It can also use pyruvate as substrate.
CC {ECO:0000269|PubMed:9484901}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxobutanoate + CoA = formate + propanoyl-CoA;
CC Xref=Rhea:RHEA:28054, ChEBI:CHEBI:15740, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392;
CC Evidence={ECO:0000269|PubMed:9484901};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28055;
CC Evidence={ECO:0000269|PubMed:9484901};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + formate = CoA + pyruvate; Xref=Rhea:RHEA:11844,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15740, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.1.54;
CC Evidence={ECO:0000269|PubMed:9484901};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11846;
CC Evidence={ECO:0000269|PubMed:9484901};
CC -!- ACTIVITY REGULATION: Dependent on PFL-activase.
CC {ECO:0000269|PubMed:9484901}.
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate
CC pathway; propanoate from L-threonine: step 2/4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Strongly repressed by glucose. Anaerobic growth of the pfl
CC mutant in the presence of cAMP and L-threonine induced synthesis of
CC TdcE. {ECO:0000269|PubMed:9484901}.
CC -!- DISRUPTION PHENOTYPE: No discernible phenotype.
CC {ECO:0000269|PubMed:9484901}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57918.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA57918.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48170.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77162.1; -; Genomic_DNA.
DR PIR; G65100; G65100.
DR RefSeq; WP_000861734.1; NZ_STEB01000001.1.
DR RefSeq; YP_026205.1; NC_000913.3.
DR AlphaFoldDB; P42632; -.
DR SMR; P42632; -.
DR BioGRID; 4262415; 15.
DR DIP; DIP-10972N; -.
DR IntAct; P42632; 2.
DR STRING; 511145.b3114; -.
DR jPOST; P42632; -.
DR PaxDb; P42632; -.
DR PRIDE; P42632; -.
DR EnsemblBacteria; AAT48170; AAT48170; b3114.
DR EnsemblBacteria; BAE77162; BAE77162; BAE77162.
DR GeneID; 66672985; -.
DR GeneID; 947623; -.
DR KEGG; ecj:JW5522; -.
DR KEGG; eco:b3114; -.
DR PATRIC; fig|1411691.4.peg.3616; -.
DR EchoBASE; EB2612; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_023898_0_0_6; -.
DR InParanoid; P42632; -.
DR OMA; MNTIHYM; -.
DR PhylomeDB; P42632; -.
DR BioCyc; EcoCyc:KETOBUTFORMLY-INACT-MON; -.
DR BioCyc; MetaCyc:KETOBUTFORMLY-INACT-MON; -.
DR UniPathway; UPA00052; UER00508.
DR PRO; PR:P42632; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR GO; GO:0043875; F:2-ketobutyrate formate-lyase activity; IGI:EcoliWiki.
DR GO; GO:0008861; F:formate C-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0070689; P:L-threonine catabolic process to propionate; IC:EcoliWiki.
DR GO; GO:0006567; P:threonine catabolic process; IEP:EcoCyc.
DR CDD; cd01678; PFL1; 1.
DR InterPro; IPR005949; Form_AcTrfase.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
DR Pfam; PF01228; Gly_radical; 1.
DR Pfam; PF02901; PFL-like; 1.
DR TIGRFAMs; TIGR01255; pyr_form_ly_1; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
DR PROSITE; PS51554; PFL; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Organic radical; Reference proteome;
KW Transferase.
FT CHAIN 1..764
FT /note="PFL-like enzyme TdcE"
FT /id="PRO_0000166691"
FT DOMAIN 7..629
FT /note="PFL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT DOMAIN 636..764
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT REGION 622..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 423
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 424
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 739
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 764 AA; 85936 MW; 2C4F46944118449B CRC64;
MKVDIDTSDK LYADAWLGFK GTDWKNEINV RDFIQHNYTP YEGDESFLAE ATPATTELWE
KVMEGIRIEN ATHAPVDFDT NIATTITAHD AGYINQPLEK IVGLQTDAPL KRALHPFGGI
NMIKSSFHAY GREMDSEFEY LFTDLRKTHN QGVFDVYSPD MLRCRKSGVL TGLPDGYGRG
RIIGDYRRVA LYGISYLVRE RELQFADLQS RLEKGEDLEA TIRLREELAE HRHALLQIQE
MAAKYGFDIS RPAQNAQEAV QWLYFAYLAA VKSQNGGAMS LGRTASFLDI YIERDFKAGV
LNEQQAQELI DHFIMKIRMV RFLRTPEFDS LFSGDPIWAT EVIGGMGLDG RTLVTKNSFR
YLHTLHTMGP APEPNLTILW SEELPIAFKK YAAQVSIVTS SLQYENDDLM RTDFNSDDYA
IACCVSPMVI GKQMQFFGAR ANLAKTLLYA INGGVDEKLK IQVGPKTAPL MDDVLDYDKV
MDSLDHFMDW LAVQYISALN IIHYMHDKYS YEASLMALHD RDVYRTMACG IAGLSVATDS
LSAIKYARVK PIRDENGLAV DFEIDGEYPQ YGNNDERVDS IACDLVERFM KKIKALPTYR
NAVPTQSILT ITSNVVYGQK TGNTPDGRRA GTPFAPGANP MHGRDRKGAV ASLTSVAKLP
FTYAKDGISY TFSIVPAALG KEDPVRKTNL VGLLDGYFHH EADVEGGQHL NVNVMNREML
LDAIEHPEKY PNLTIRVSGY AVRFNALTRE QQQDVISRTF TQAL
