4HYPE_XANCP
ID 4HYPE_XANCP Reviewed; 312 AA.
AC Q8P833;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=4-hydroxyproline 2-epimerase {ECO:0000303|PubMed:24980702};
DE Short=4Hyp 2-epimerase;
DE Short=4HypE {ECO:0000303|PubMed:24980702};
DE EC=5.1.1.8 {ECO:0000269|PubMed:24980702};
GN OrderedLocusNames=XCC2415 {ECO:0000312|EMBL:AAM41693.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH AN UNKNOWN LIGAND,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24980702; DOI=10.7554/elife.03275;
RA Zhao S., Sakai A., Zhang X., Vetting M.W., Kumar R., Hillerich B.,
RA San Francisco B., Solbiati J., Steves A., Brown S., Akiva E., Barber A.,
RA Seidel R.D., Babbitt P.C., Almo S.C., Gerlt J.A., Jacobson M.P.;
RT "Prediction and characterization of enzymatic activities guided by sequence
RT similarity and genome neighborhood networks.";
RL Elife 3:E03275-E03275(2014).
CC -!- FUNCTION: Catalyzes the epimerization of trans-4-hydroxy-L-proline
CC (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a
CC degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can
CC also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp)
CC to cis-3-hydroxy-D-proline (c3DHyp), albeit with 500-fold lower
CC efficiency. Displays no proline racemase activity.
CC {ECO:0000269|PubMed:24980702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline;
CC Xref=Rhea:RHEA:21152, ChEBI:CHEBI:57690, ChEBI:CHEBI:58375;
CC EC=5.1.1.8; Evidence={ECO:0000269|PubMed:24980702};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.67 mM for trans-4-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC KM=15 mM for trans-3-hydroxy-L-proline {ECO:0000269|PubMed:24980702};
CC Note=kcat is 28 sec(-1) for t4LHyp epimerization. kcat is 1.3 sec(-1)
CC for t3LHyp epimerization. {ECO:0000269|PubMed:24980702};
CC -!- SIMILARITY: Belongs to the proline racemase family. {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; AE008922; AAM41693.1; -; Genomic_DNA.
DR RefSeq; NP_637769.1; NC_003902.1.
DR RefSeq; WP_011037557.1; NC_003902.1.
DR PDB; 4JUU; X-ray; 1.75 A; A/B=1-312.
DR PDBsum; 4JUU; -.
DR AlphaFoldDB; Q8P833; -.
DR SMR; Q8P833; -.
DR STRING; 340.xcc-b100_1751; -.
DR EnsemblBacteria; AAM41693; AAM41693; XCC2415.
DR KEGG; xcc:XCC2415; -.
DR PATRIC; fig|190485.4.peg.2575; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_1_0_6; -.
DR OMA; SHVLWTG; -.
DR SABIO-RK; Q8P833; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0047580; F:4-hydroxyproline epimerase activity; IDA:CACAO.
DR InterPro; IPR008794; Pro_racemase_fam.
DR PANTHER; PTHR33442; PTHR33442; 1.
DR Pfam; PF05544; Pro_racemase; 1.
DR PIRSF; PIRSF029792; Pro_racemase; 1.
DR SFLD; SFLDS00028; Proline_Racemase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..312
FT /note="4-hydroxyproline 2-epimerase"
FT /id="PRO_0000432246"
FT ACT_SITE 88
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT ACT_SITE 238
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 89..90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 239..240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT STRAND 1..11
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:4JUU"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:4JUU"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:4JUU"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4JUU"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 136..147
FT /evidence="ECO:0007829|PDB:4JUU"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 151..168
FT /evidence="ECO:0007829|PDB:4JUU"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4JUU"
FT HELIX 179..196
FT /evidence="ECO:0007829|PDB:4JUU"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:4JUU"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:4JUU"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:4JUU"
FT STRAND 290..300
FT /evidence="ECO:0007829|PDB:4JUU"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:4JUU"
SQ SEQUENCE 312 AA; 32711 MW; FC113653AE768D37 CRC64;
MHTIDVIDSH TAGEPTRVVL AGFPDLGDGD LAQCRERFRS DFDHWRSAIA CEPRGSDTMV
GALLLPPRDP SACTGVIFFN NVGYLGMCGH GTIGVVRTLA ELGRIAPGQH RIETPVGTVG
VALADDGTVS IDNVESYRHA AGVEVDVPGH GRVRGDVAWG GNWFFITEQA PCALGLAQQR
ELTAYTEAIR LALEAAGITG EAGGEIDHIE ISGVAPDGSG AARNFVLCPG LAYDRSPCGT
GTSAKLACLA ADGKLAEGER WLQQGILGSA FEGSYRHSGR GIAPRISGHA FITARSQLLI
DPADPFAWGI VA
