ID   PROHY_STRGD             Reviewed;         268 AA.
AC   R9UTQ8;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=L-proline trans-4-hydroxylase {ECO:0000303|PubMed:6324794};
DE            Short=P4H {ECO:0000303|PubMed:8546682};
DE            EC=1.14.11.57 {ECO:0000269|PubMed:8546682, ECO:0000305|PubMed:6324794};
OS   Streptomyces griseoviridis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=45398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=23161816; DOI=10.1002/cbic.201200584;
RA   Xie Y., Wang B., Liu J., Zhou J., Ma J., Huang H., Ju J.;
RT   "Identification of the biosynthetic gene cluster and regulatory cascade for
RT   the synergistic antibacterial antibiotics griseoviridin and viridogrisein
RT   in Streptomyces griseoviridis.";
RL   ChemBioChem 13:2745-2757(2012).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, AND COFACTOR.
RX   PubMed=6324794; DOI=10.1016/0006-291x(84)91411-6;
RA   Onishi M., Okumura Y., Okamoto R., Ishikura T.;
RT   "Proline hydroxylation by cell free extract of a streptomycete.";
RL   Biochem. Biophys. Res. Commun. 120:45-51(1984).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, COFACTOR, PATHWAY, AND SUBUNIT.
RC   STRAIN=P8648;
RX   PubMed=8546682; DOI=10.1042/bj3130185;
RA   Lawrence C.C., Sobey W.J., Field R.A., Baldwin J.E., Schofield C.J.;
RT   "Purification and initial characterization of proline 4-hydroxylase from
RT   Streptomyces griseoviridus P8648: a 2-oxoacid, ferrous-dependent
RT   dioxygenase involved in etamycin biosynthesis.";
RL   Biochem. J. 313:185-191(1996).
CC   -!- FUNCTION: Involved in the biosynthesis of the peptidolactone antibiotic
CC       etamycin (viridogrisein) (PubMed:6324794, PubMed:8546682). Catalyzes
CC       the hydroxylation of free L-proline at the C-4 position to yield trans-
CC       4-hydroxy-L-proline (PubMed:6324794, PubMed:8546682).
CC       {ECO:0000269|PubMed:6324794, ECO:0000269|PubMed:8546682}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-proline + O2 = CO2 + succinate + trans-4-
CC         hydroxy-L-proline; Xref=Rhea:RHEA:51508, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:58375, ChEBI:CHEBI:60039; EC=1.14.11.57;
CC         Evidence={ECO:0000269|PubMed:8546682, ECO:0000305|PubMed:6324794};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:6324794, ECO:0000269|PubMed:8546682};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000250|UniProtKB:Q2TDY4};
CC   -!- ACTIVITY REGULATION: Competitively inhibited by pyridine-2,4-
CC       dicarboxylate (PubMed:8546682). Inhibited by diethyl pyrocarbonate
CC       (DEPC), 3,4-dihydroxybenzoate, pyridine-2,5-dicarboxylate,
CC       alpha,alpha'-dipyridyl, and some metal ions such as Co(2+) and Zn(2+)
CC       (PubMed:6324794, PubMed:8546682). {ECO:0000269|PubMed:6324794,
CC       ECO:0000269|PubMed:8546682}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=32 uM for 2-oxoglutarate {ECO:0000269|PubMed:8546682};
CC         KM=445 uM for L-proline {ECO:0000269|PubMed:8546682};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:6324794};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.
CC         {ECO:0000269|PubMed:6324794};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:8546682}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8546682}.
CC   -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR   EMBL; JX508597; AGN74870.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9UTQ8; -.
DR   SMR; R9UTQ8; -.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016999; P:antibiotic metabolic process; IDA:UniProtKB.
DR   InterPro; IPR008775; Phytyl_CoA_dOase.
DR   Pfam; PF05721; PhyH; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..268
FT                   /note="L-proline trans-4-hydroxylase"
FT                   /id="PRO_0000445005"
FT   BINDING         113
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT   BINDING         115
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT   BINDING         218
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
SQ   SEQUENCE   268 AA;  29603 MW;  3AF4E111D558999F CRC64;
     MSVSAPLLDA KVRYGRDGWL PLPHTLSDPD VRKLRQRIEG ISREQRPEVV LEEGSSAVRA
     LHGCHDFDEV CARLVRLPAL VGLAEQLLGG PVYVYQFKVN MKQAHEGAAW PWHQDFAFWH
     HEDGMGAPDA VNIAIFLDDV TDENGPLEVI PGSQHAGIVE DTARPGRERS HDWRHHVSAK
     LEYVVPDEIA GRLAGTFGVR RLTGPAGTAV AFHPSIIHSS SNNTSAQRRC VLLITYNRVT
     NTPAHPVRPP FLVSRDSTPV VPVDADRL