PRPE_ECOLI
ID PRPE_ECOLI Reviewed; 628 AA.
AC P77495; Q2MC89;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Propionate--CoA ligase;
DE EC=6.2.1.17;
DE AltName: Full=Propionyl-CoA synthetase;
GN Name=prpE; Synonyms=yahU; OrderedLocusNames=b0335, JW0326;
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;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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).
CC -!- FUNCTION: Catalyzes the synthesis of propionyl-CoA from propionate and
CC CoA. Also converts acetate to acetyl-CoA but with a lower specific
CC activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456215; EC=6.2.1.17;
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; U73857; AAB18059.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73438.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76117.1; -; Genomic_DNA.
DR PIR; G64760; G64760.
DR RefSeq; NP_414869.1; NC_000913.3.
DR RefSeq; WP_000010288.1; NZ_LN832404.1.
DR AlphaFoldDB; P77495; -.
DR SMR; P77495; -.
DR BioGRID; 4259811; 7.
DR IntAct; P77495; 7.
DR STRING; 511145.b0335; -.
DR PaxDb; P77495; -.
DR PRIDE; P77495; -.
DR EnsemblBacteria; AAC73438; AAC73438; b0335.
DR EnsemblBacteria; BAE76117; BAE76117; BAE76117.
DR GeneID; 946891; -.
DR KEGG; ecj:JW0326; -.
DR KEGG; eco:b0335; -.
DR PATRIC; fig|1411691.4.peg.1942; -.
DR EchoBASE; EB3372; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_5_6; -.
DR InParanoid; P77495; -.
DR OMA; YSSLDWA; -.
DR PhylomeDB; P77495; -.
DR BioCyc; EcoCyc:G6200-MON; -.
DR BioCyc; MetaCyc:G6200-MON; -.
DR BRENDA; 6.2.1.17; 2026.
DR UniPathway; UPA00946; -.
DR PRO; PR:P77495; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IDA:EcoCyc.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR012694; Propion_PrpE.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02316; propion_prpE; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..628
FT /note="Propionate--CoA ligase"
FT /id="PRO_0000193188"
SQ SEQUENCE 628 AA; 69351 MW; B192E2E49ED900D8 CRC64;
MSFSEFYQRS INEPEQFWAE QARRIDWQTP FTQTLDHSNP PFARWFCEGR TNLCHNAIDR
WLEKQPEALA LIAVSSETEE ERTFTFRQLH DEVNAVASML RSLGVQRGDR VLVYMPMIAE
AHITLLACAR IGAIHSVVFG GFASHSVAAR IDDAKPVLIV SADAGARGGK IIPYKKLLDD
AISQAQHQPR HVLLVDRGLA KMARVSGRDV DFASLRHQHI GARVPVAWLE SNETSCILYT
SGTTGKPKGV QRDVGGYAVA LATSMDTIFG GKAGSVFFCA SDIGWVVGHS YIVYAPLLAG
MATIVYEGLP TWPDCGVWWT IVEKYQVSRM FSAPTAIRVL KKFPTAEIRK HDLSSLEVLY
LAGEPLDEPT ASWVSNTLDV PVIDNYWQTE SGWPIMAIAR GLDDRPTRLG SPGVPMYGYN
VQLLNEVTGE PCGVNEKGML VVEGPLPPGC IQTIWGDDGR FVKTYWSLFS RPVYATFDWG
IRDADGYHFI LGRTDDVINV AGHRLGTREI EESISSHPGV AEVAVVGVKD ALKGQVAVAF
VIPKESDSLE DRDVAHSQEK AIMALVDSQI GNFGRPAHVW FVSQLPKTRS GKMLRRTIQA
ICEGRDPGDL TTIDDPASLD QIRQAMEE
