(data stored in ACNUC7421 zone)

SWISSPROT: MHPA_SHISS

ID   MHPA_SHISS              Reviewed;         554 AA.
AC   Q3Z585;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase {ECO:0000255|HAMAP-Rule:MF_01652};
DE            Short=3-HCI hydroxylase {ECO:0000255|HAMAP-Rule:MF_01652};
DE            Short=3-HPP hydroxylase {ECO:0000255|HAMAP-Rule:MF_01652};
DE            EC=1.14.13.127 {ECO:0000255|HAMAP-Rule:MF_01652};
GN   Name=mhpA {ECO:0000255|HAMAP-Rule:MF_01652};
GN   OrderedLocusNames=SSON_0297;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Catalyzes the insertion of one atom of molecular oxygen
CC       into position 2 of the phenyl ring of 3-(3-
CC       hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI).
CC       {ECO:0000255|HAMAP-Rule:MF_01652}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-(3-hydroxyphenyl)propanoate + H(+) + NADH + O2 = 3-
CC         (2,3-dihydroxyphenyl)propanoate + H2O + NAD(+);
CC         Xref=Rhea:RHEA:24785, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:46951, ChEBI:CHEBI:57277,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.127;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01652};
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01652};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01652};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate
CC       degradation. {ECO:0000255|HAMAP-Rule:MF_01652}.
CC   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01652}.
DR   EMBL; CP000038; AAZ87077.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87077; AAZ87077; SSON_0297.
DR   KEGG; ssn:SSON_0297; -.
DR   HOGENOM; HOG000221401; -.
DR   KO; K05712; -.
DR   OMA; YTFQCRR; -.
DR   BioCyc; SSON300269:G1GL2-342-MONOMER; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0008688; F:3-(3-hydroxyphenyl)propionate hydroxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0019622; P:3-(3-hydroxy)phenylpropionate catabolic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; Q3Z585.
DR   SWISS-2DPAGE; Q3Z585.
KW   Aromatic hydrocarbons catabolism; Complete proteome; FAD;
KW   Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN         1    554       3-(3-hydroxy-phenyl)propionate/3-
FT                                hydroxycinnamic acid hydroxylase.
FT                                /FTId=PRO_0000337643.
FT   NP_BIND      17     46       FAD. {ECO:0000255|HAMAP-Rule:MF_01652}.
FT   NP_BIND     285    295       FAD. {ECO:0000255|HAMAP-Rule:MF_01652}.
SQ   SEQUENCE   554 AA;  62150 MW;  1869C3AF73889075 CRC64;
     MAIQHPDIQP AVNHSVQVAI AGAGPVGLMM ANYLGQMGID VLVVEKLDKL IDYPRAIGID
     DEALRTMQSV GLVENVLPHT TPWHAMRFLT PKGRCFADIQ PMTDEFGWPR RNAFIQPQVD
     AVMLEGLSRF PNVRCLFSRE LEAFSQQDDE VTLHLKTAEG QRETIKAQWL VACDGGASFV
     RRTLNVPFEG KTAPNQWIVV DIANDPLSTP HIYLCCDPVR PYVSAALPHA VRRFEFMVMP
     GETEEQLREP QNMRKLLSKV LPNPDNVELI RQRVYTHNAR LAQRFRIDRV LLAGDAAHIM
     PVWQGQGYNS GMRDAFNLAW KLALVIQGKA RDALLDTYQQ ERRDHAKAMI DLSVTAGNVL
     APPKRWQGTL RDGVSWLLNY LPPVKRYFLE MRFKPMPQYY GGALVREGEA KHSPVGKMFI
     QPKVTLENGD VTLLDNAIGA NFAVIGWGCN PLWGMSDEQI QQWRALGTRF IQVVPEVQIH
     TAQDNHDGVL HVGDTQGRLR SWFAQHNASL VVMRPDRFVA ATAIPQTLGN TLNKLASVMT
     LTRPDADVSV EKVA
//

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