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MHPA_ECOLI
ID   MHPA_ECOLI              Reviewed;         554 AA.
AC   P77397; P71203; P77047; Q2MC77;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
DE            Short=3-HCI hydroxylase;
DE            Short=3-HPP hydroxylase;
DE            EC=1.14.13.127;
GN   Name=mhpA; OrderedLocusNames=b0347, JW0338;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Kawamukai M.;
RT   "Complete sequence of the mhp operon.";
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / CS520;
RX   PubMed=9098055; DOI=10.1128/jb.179.8.2573-2581.1997;
RA   Ferrandez A., Garcia J.L., Diaz E.;
RT   "Genetic characterization and expression in heterologous hosts of the 3-(3-
RT   hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12.";
RL   J. Bacteriol. 179:2573-2581(1997).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   FUNCTION IN CATABOLISM OF 3-HYDROXY DERIVATIVES OF PHENYLPROPIONIC ACID.
RX   PubMed=9603882; DOI=10.1128/jb.180.11.2915-2923.1998;
RA   Diaz E., Ferrandez A., Garcia J.L.;
RT   "Characterization of the hca cluster encoding the dioxygenolytic pathway
RT   for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-
RT   12.";
RL   J. Bacteriol. 180:2915-2923(1998).
CC   -!- FUNCTION: Catalyzes the insertion of one atom of molecular oxygen into
CC       position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP)
CC       and hydroxycinnamic acid (3HCI). {ECO:0000269|PubMed:9603882}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-(3-hydroxyphenyl)propanoate + H(+) + NADH + O2 = 3-(2,3-
CC         dihydroxyphenyl)propanoate + H2O + NAD(+); Xref=Rhea:RHEA:24785,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:46951, ChEBI:CHEBI:57277, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.14.13.127;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-3-(3-hydroxyphenyl)prop-2-enoate + H(+) + NADH + O2 =
CC         (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + H2O + NAD(+);
CC         Xref=Rhea:RHEA:27846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:47928, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58642; EC=1.14.13.127;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; D86239; BAA13052.1; -; Genomic_DNA.
DR   EMBL; Y09555; CAA70747.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18071.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73450.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76129.1; -; Genomic_DNA.
DR   PIR; C64762; C64762.
DR   RefSeq; NP_414881.1; NC_000913.3.
DR   RefSeq; WP_001007407.1; NZ_SSZK01000061.1.
DR   AlphaFoldDB; P77397; -.
DR   SMR; P77397; -.
DR   BioGRID; 4260728; 15.
DR   BioGRID; 849583; 1.
DR   IntAct; P77397; 3.
DR   STRING; 511145.b0347; -.
DR   PaxDb; P77397; -.
DR   PRIDE; P77397; -.
DR   EnsemblBacteria; AAC73450; AAC73450; b0347.
DR   EnsemblBacteria; BAE76129; BAE76129; BAE76129.
DR   GeneID; 945197; -.
DR   KEGG; ecj:JW0338; -.
DR   KEGG; eco:b0347; -.
DR   PATRIC; fig|1411691.4.peg.1931; -.
DR   EchoBASE; EB4166; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_009665_20_2_6; -.
DR   InParanoid; P77397; -.
DR   OMA; FHSDERQ; -.
DR   PhylomeDB; P77397; -.
DR   BioCyc; EcoCyc:MHPHYDROXY-MON; -.
DR   BioCyc; MetaCyc:MHPHYDROXY-MON; -.
DR   UniPathway; UPA00714; -.
DR   PRO; PR:P77397; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008688; F:3-(3-hydroxyphenyl)propionate hydroxylase activity; IDA:EcoCyc.
DR   GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0019622; P:3-(3-hydroxy)phenylpropionate catabolic process; IMP:EcoCyc.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_01652; MhpA; 1.
DR   InterPro; IPR023786; 3-HPP/3HCI_hydroxylase.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..554
FT                   /note="3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic
FT                   acid hydroxylase"
FT                   /id="PRO_0000214043"
FT   BINDING         17..46
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         285..295
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        272
FT                   /note="Q -> H (in Ref. 1; BAA13052)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360
FT                   /note="L -> P (in Ref. 1; BAA13052)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        502
FT                   /note="W -> G (in Ref. 1; BAA13052)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   554 AA;  62186 MW;  1D56CB799E9F8A8E CRC64;
     MAIQHPDIQP AVNHSVQVAI AGAGPVGLMM ANYLGQMGID VLVVEKLDKL IDYPRAIGID
     DEALRTMQSV GLVDDVLPHT TPWHAMRFLT PKGRCFADIQ PMTDEFGWPR RNAFIQPQVD
     AVMLEGVSRF PNVRCLFSRE LEAFSQQDDE VTLHLKTAEG QREIVKAQWL VACDGGASFV
     RRTLNVPFEG KTAPNQWIVV DIANDPLSTP HIYLCCDPVR PYVSAALPHA VRRFEFMVMP
     GETEEQLREP QNMRKLLSKV LPNPDNVELI RQRVYTHNAR LAQRFRIDRV LLAGDAAHIM
     PVWQGQGYNS GMRDAFNLAW KLALVIQGKA RDALLDTYQQ ERRDHAKAMI DLSVTAGNVL
     APPKRWQGTL RDGVSWLLNY LPPVKRYFLE MRFKPMPQYY GGALMREGEA KHSPVGKMFI
     QPKVTLENGD VTLLDNAIGA NFAVIGWGCN PLWGMSDEQI QQWRALGTRF IQVVPEVQIH
     TAQDNHDGVL RVGDTQGRLR SWFAQHNASL VVMRPDRFVA ATAIPQTLGK TLNKLASVMT
     LTRPDADVSV EKVA
 
 
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