P3H2_STRSQ
ID P3H2_STRSQ Reviewed; 290 AA.
AC O09345;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=L-proline cis-3-hydroxylase 2;
DE Short=P3H 2;
DE EC=1.14.11.28;
DE AltName: Full=Proline 3-hydroxylase 2;
DE AltName: Full=Proline 3-hydroxylase type II;
OS Streptomyces sp.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1931;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=TH1 / FERM BP-4399;
RA Shibasaki T., Mori H., Ozaki A.;
RT "Cloning of an isozyme of proline 3-hydroxylase and its purification from
RT recombinant Escherichia coli.";
RL Biotechnol. Lett. 22:1967-1973(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP FE(2+), SUBUNIT, AND REACTION MECHANISM.
RX PubMed=11737217; DOI=10.1046/j.0014-2956.2001.02617.x;
RA Clifton I.J., Hsueh L.C., Baldwin J.E., Harlos K., Schofield C.J.;
RT "Structure of proline 3-hydroxylase. Evolution of the family of 2-
RT oxoglutarate dependent oxygenases.";
RL Eur. J. Biochem. 268:6625-6636(2001).
CC -!- FUNCTION: Dioxygenase that catalyzes the 2-oxoglutarate-dependent
CC selective hydroxylation of free L-proline to cis-3-hydroxy-L-proline
CC (cis-3-Hyp). {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-proline + O2 = cis-3-hydroxy-L-proline +
CC CO2 + succinate; Xref=Rhea:RHEA:20265, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:60039, ChEBI:CHEBI:60041; EC=1.14.11.28;
CC Evidence={ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|Ref.1};
CC Note=Binds 1 Fe(2+) ion. {ECO:0000269|Ref.1};
CC -!- ACTIVITY REGULATION: Inhibited by metal ions such as Co(2+), Zn(2+),
CC Ni(2+) or Cu(2+). Is also inhibited by EDTA in vitro.
CC {ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.43 mM for L-proline {ECO:0000269|Ref.1};
CC KM=0.047 mM for 2-oxoglutarate {ECO:0000269|Ref.1};
CC Note=Comparison of both proline 3-hydroxylase isozymes shows that
CC type II enzyme has 1.8-fold higher activity than type I upon L-
CC proline, and 24-fold higher activity upon L-2-azetidinecarboxylic
CC acid.;
CC pH dependence:
CC Optimum pH is 6.0. Is stable from pH 5.5 to 9.0. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius. Is stable below 40 degrees
CC Celsius. {ECO:0000269|Ref.1};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11737217}.
CC -!- SIMILARITY: Belongs to the L-proline cis-4-/cis-3-hydroxylase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF003371; AAB60894.1; -; Genomic_DNA.
DR PDB; 1E5R; X-ray; 2.30 A; A/B=1-290.
DR PDB; 1E5S; X-ray; 2.40 A; A/B=1-290.
DR PDBsum; 1E5R; -.
DR PDBsum; 1E5S; -.
DR AlphaFoldDB; O09345; -.
DR SMR; O09345; -.
DR EvolutionaryTrace; O09345; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033763; F:proline 3-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0018193; P:peptidyl-amino acid modification; IEA:InterPro.
DR Gene3D; 1.10.1720.10; -; 1.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR007803; Asp/Arg/Pro-Hydrxlase.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR008035; Pro_3_hydrox_C.
DR InterPro; IPR037037; Pro_3_hydrox_C_sf.
DR Pfam; PF05118; Asp_Arg_Hydrox; 1.
DR Pfam; PF05373; Pro_3_hydrox_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..290
FT /note="L-proline cis-3-hydroxylase 2"
FT /id="PRO_0000393427"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 158
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 168
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1E5R"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:1E5R"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:1E5R"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:1E5R"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:1E5R"
FT STRAND 88..107
FT /evidence="ECO:0007829|PDB:1E5R"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:1E5R"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1E5R"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1E5R"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1E5R"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:1E5R"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:1E5R"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:1E5R"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1E5R"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1E5R"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:1E5R"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:1E5R"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1E5R"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:1E5R"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:1E5R"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:1E5R"
FT HELIX 262..276
FT /evidence="ECO:0007829|PDB:1E5R"
SQ SEQUENCE 290 AA; 33574 MW; C571E1DAB598AE1A CRC64;
MRSHILGKIE LDQTRLAPDL AYLAAVPTVE EEYDEFSNGF WKHVPLWNAS GDSEDRLYRD
LKDAAAQPTA HVEHVPYLKE IVTTVFDGTH LQMARSRNLK NAIVIPHRDF VELDREVDRY
FRTFMVLEDS PLAFHSNEDT VIHMRPGEIW FLDAATVHSA VNFSEISRQS LCVDFAFDGP
FDEKEIFADA TLYAPGSTPD LPERRPFTAE HRRRILSLGQ VIERENFRDI LFLLSKVHYK
YDVHPSETYD WLIEISKQAG DEKMVVKAEQ IRDFAVEARA LSERFSLTSW
