ID   P3H1_STRSQ              Reviewed;         290 AA.
AC   P96010;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=L-proline cis-3-hydroxylase 1;
DE            Short=P3H 1;
DE            EC=1.14.11.28;
DE   AltName: Full=Proline 3-hydroxylase 1;
DE   AltName: Full=Proline 3-hydroxylase type I;
OS   Streptomyces sp.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-29; 43-67 AND
RP   185-209, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP   SUBSTRATE SPECIFICITY.
RC   STRAIN=TH1 / FERM BP-4399;
RX   PubMed=9294421; DOI=10.1128/jb.179.18.5677-5683.1997;
RA   Mori H., Shibasaki T., Yano K., Ozaki A.;
RT   "Purification and cloning of a proline 3-hydroxylase, a novel enzyme which
RT   hydroxylates free L-proline to cis-3-hydroxy-L-proline.";
RL   J. Bacteriol. 179:5677-5683(1997).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE 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).
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). D-proline, trans-4-hydroxy-L-proline, cis-4-hydroxy-L-
CC       proline, cis-4-hydroxy-D-proline, and 3,4-dehydro-DL-proline are not
CC       substrates. {ECO:0000269|PubMed:9294421, ECO:0000269|Ref.2}.
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|PubMed:9294421, ECO:0000269|Ref.2};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:9294421, ECO:0000269|Ref.2};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000269|PubMed:9294421,
CC       ECO:0000269|Ref.2};
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. Unlike the
CC       procollagen-proline cis-3- and trans-4-hydroxylases from mammals, does
CC       not necessarily require L-ascorbate for activity although it does
CC       increase the activity of the enzyme. {ECO:0000269|PubMed:9294421,
CC       ECO:0000269|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.20 mM for L-proline {ECO:0000269|Ref.2};
CC         KM=0.083 mM for 2-oxoglutarate {ECO:0000269|Ref.2};
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 8.5. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius. Is stable below 30 degrees
CC         Celsius. {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; AB007189; BAA22406.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96010; -.
DR   SMR; P96010; -.
DR   KEGG; ag:BAA22406; -.
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   Dioxygenase; Direct protein sequencing; Iron; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..290
FT                   /note="L-proline cis-3-hydroxylase 1"
FT                   /id="PRO_0000393426"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   290 AA;  33154 MW;  7AC1A538D0FB294C CRC64;
     MRSHILGRIE LDQERLGRDL EYLATVPTVE EEYDEFSNGF WKNIPLYNAS GGSEDRLYRD
     LEGSPAQPTK HAEQVPYLNE IITTVYNGER LQMARTRNLK NAVVIPHRDF VELDRELDQY
     FRTHLMLEDS PLAFHSDDDT VIHMRAGEIW FLDAAAVHSA VNFAEFSRQS LCVDLAFDGA
     FDEKEAFADA TVYAPNLSPD VRERKPFTKE REAGILALSG VIGRENFRDI LFLLSKVHYT
     YDVHPGETFE WLVSVSKGAG DDKMVEKAER IRDFAIGARA LGERFSLTTW