P4H_RHIME
ID P4H_RHIME Reviewed; 280 AA.
AC Q92LF6;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=L-proline cis-4-hydroxylase;
DE Short=P4H;
DE EC=1.14.11.56 {ECO:0000269|PubMed:19133227};
GN OrderedLocusNames=R03107; ORFNames=SMc03253;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=MAFF303099;
RX PubMed=19133227; DOI=10.1016/j.bbrc.2008.12.158;
RA Hara R., Kino K.;
RT "Characterization of novel 2-oxoglutarate dependent dioxygenases converting
RT L-proline to cis-4-hydroxy-l-proline.";
RL Biochem. Biophys. Res. Commun. 379:882-886(2009).
CC -!- FUNCTION: Dioxygenase that catalyzes the 2-oxoglutarate-dependent
CC selective hydroxylation of free L-proline to cis-4-hydroxy-L-proline
CC (cis-4-Hyp). {ECO:0000269|PubMed:19133227}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-proline + O2 = cis-4-hydroxy-L-proline +
CC CO2 + succinate; Xref=Rhea:RHEA:32127, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:60039, ChEBI:CHEBI:63727; EC=1.14.11.56;
CC Evidence={ECO:0000269|PubMed:19133227};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:19133227};
CC Note=Binds 1 Fe(2+) ion. {ECO:0000269|PubMed:19133227};
CC -!- ACTIVITY REGULATION: Inhibited by metal ions such as Co(2+), Zn(2+),
CC Cu(2+) or Ni(2+). Is also inhibited by EDTA or diethylpyrocarbonate
CC (DEPC) in vitro. Unlike the procollagen-proline cis-3- and trans-4-
CC hydroxylases from mammals, does not necessarily require L-ascorbate for
CC activity although it does increase the activity of the enzyme.
CC {ECO:0000269|PubMed:19133227}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.54 mM for L-proline {ECO:0000269|PubMed:19133227};
CC KM=0.30 mM for 2-oxoglutarate {ECO:0000269|PubMed:19133227};
CC Note=kcat is 25 sec(-1).;
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:19133227};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:19133227};
CC -!- BIOTECHNOLOGY: Would be one of the most promising biocatalysts for
CC production of cis-4-hydroxy-L-proline (cis-4-Hyp), a compound which was
CC clinically evaluated as an anticancer drug.
CC {ECO:0000269|PubMed:19133227}.
CC -!- SIMILARITY: Belongs to the L-proline cis-4-/cis-3-hydroxylase family.
CC {ECO:0000305}.
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DR EMBL; AL591688; CAC47686.1; -; Genomic_DNA.
DR RefSeq; NP_387213.1; NC_003047.1.
DR RefSeq; WP_010970414.1; NC_003047.1.
DR AlphaFoldDB; Q92LF6; -.
DR SMR; Q92LF6; -.
DR STRING; 266834.SMc03253; -.
DR EnsemblBacteria; CAC47686; CAC47686; SMc03253.
DR GeneID; 61604569; -.
DR KEGG; sme:SMc03253; -.
DR PATRIC; fig|266834.11.peg.4644; -.
DR eggNOG; COG3555; Bacteria.
DR HOGENOM; CLU_962849_0_0_5; -.
DR OMA; EIWFLDA; -.
DR BRENDA; 1.14.11.56; 3243.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..280
FT /note="L-proline cis-4-hydroxylase"
FT /id="PRO_0000393425"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255"
SQ SEQUENCE 280 AA; 32022 MW; 9521ABD622C7AF2C CRC64;
MSTHFLGKVK FDEARLAEDL STLEVAEFSS AYSDFACGKW EACVLRNRTG MQEEDIVVSH
NAPALATPLS KSLPYLNELV ETHFDCSAVR YTRIVRVSEN ACIIPHSDYL ELDETFTRLH
LVLDTNSGCA NTEEDKIFHM GLGEIWFLDA MLPHSAACFS KTPRLHLMID FEATAFPESF
LRNVEQPVTT RDMVDPRKEL TDEVIEGILG FSIIISEANY REIVSILAKL HFFYKADCRS
MYDWLKEICK RRGDPALIEK TASLERFFLG HRERGEVMTY
