ID   OPLA_DICDI              Reviewed;        1265 AA.
AC   Q54NW6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=5-oxoprolinase;
DE            EC=3.5.2.9;
DE   AltName: Full=5-oxo-L-prolinase;
DE            Short=5-OPase;
DE   AltName: Full=Pyroglutamase;
GN   Name=oplah; ORFNames=DDB_G0284953;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalyzes the cleavage of 5-oxo-L-proline to form L-glutamate
CC       coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate +
CC         phosphate; Xref=Rhea:RHEA:10348, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58402, ChEBI:CHEBI:456216; EC=3.5.2.9;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the oxoprolinase family. {ECO:0000305}.
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DR   EMBL; AAFI02000073; EAL64940.2; -; Genomic_DNA.
DR   RefSeq; XP_639951.2; XM_634859.2.
DR   AlphaFoldDB; Q54NW6; -.
DR   SMR; Q54NW6; -.
DR   STRING; 44689.DDB0304678; -.
DR   PaxDb; Q54NW6; -.
DR   EnsemblProtists; EAL64940; EAL64940; DDB_G0284953.
DR   GeneID; 8624863; -.
DR   KEGG; ddi:DDB_G0284953; -.
DR   dictyBase; DDB_G0284953; oplah.
DR   eggNOG; KOG1939; Eukaryota.
DR   HOGENOM; CLU_002157_0_0_1; -.
DR   InParanoid; Q54NW6; -.
DR   OMA; TDCNVML; -.
DR   PhylomeDB; Q54NW6; -.
DR   Reactome; R-DDI-174403; Glutathione synthesis and recycling.
DR   PRO; PR:Q54NW6; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   InterPro; IPR008040; Hydant_A_N.
DR   InterPro; IPR002821; Hydantoinase_A.
DR   InterPro; IPR003692; Hydantoinase_B.
DR   InterPro; IPR045079; Oxoprolinase_fam.
DR   PANTHER; PTHR11365; PTHR11365; 1.
DR   Pfam; PF05378; Hydant_A_N; 1.
DR   Pfam; PF01968; Hydantoinase_A; 1.
DR   Pfam; PF02538; Hydantoinase_B; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1265
FT                   /note="5-oxoprolinase"
FT                   /id="PRO_0000328515"
SQ   SEQUENCE   1265 AA;  138977 MW;  8CF76C8FB996D271 CRC64;
     MTIDKLKKSI KFNIDRGGTF TDIYAEFPYE PYYIVEKLLS VDPENYSDAP REGIRRILER
     IQGKSISKEN VDTYAIKSIR MGTTVGTNAL LERKGEKVLL VTSKGFRDLL QIGNQSRPKI
     FELNITKPEL IYNSVVELDE RVQIVTNDQV LNDIKLESPN SLKKGTTGDY IKVLEIPNRD
     KIKSELLKYF VKGIKSIAVV FIHSYTFHDH ELLVGEIAKE IGFEHISLSH QLMPMIKAVP
     RGLTSCVDAY LTPLIELYIK NFTKGFDSNI GDVDISFMMS DGGLCPVDSF RGFRSILSGP
     AGGVVGYSKT TSTVIESHKN NNGNNEIKQQ PIIGFDMGGT STDVSRYNGT LDHVFETEIS
     GLTIQAPQLD IHTVAAGGGS RLFFKSGLFL VGPESVGAHP GPVCYKKNGQ LAITDANLLL
     GRLLPEYFPP IFGPNQNEPL DLEATKKAFK ELTDEINQFQ QNNNLPLMTE DQVAFGFIRV
     ANEAMCRPIR NITEAKGFDC SQHVLACFGG AGGQHSCSIA QNLGMPKVFI HRFSGILSAY
     GLGLADLVID TQEPCSLIYN KENKSTFEKQ LNQLKENAKQ QLLNKGFPEE EIFCEGFLNL
     RFSGTDTAMM IKTPDNHDYE AEFKSNYKRE FGFLILGRDL LIDDIRVRVH ARGSDLNSLR
     INDSTGEPLK PETIQKCYFE SVGRIDTPIY LLKSLCGGDS IDGPAIIIDN TTTIVVEPNC
     KANILKPSGN IEILIGGGKS KTVTTELDPI MLSVFSHRFM SIAEQMGKII IRTSISTNIK
     ERLDFSCALF SPDGGLVANA PAIPIHVGSM QNAVKYQVET LGSNWKEGEV VLSNHPQAGG
     SHLPDLTVMT PVYHKGEIVF FVASRGHHAD IGGITPGSMP PFSKSISEEG AAIMSLKIVK
     DGHFQEEAVR KTFEKSRNLS DNISDLKAQI AANHKGIQLM QELINHYGLD VVHAYMYHIQ
     KNAELAVRDM LYDISISNNL KPLDTLISTD YMDDGSKIEL KLTIDREKKS AIFDWSGSGV
     EVYGNTNAPT SITLSATIYS LRAMVKSEIP LNQGCLAPIL TVIPPGSILN PSFDSAVVGG
     NVLTSQRLTD VILSAFGACA NSQGCMNNLT FGDETLGYYE TIAGGTGAGP NFNGFTAVQS
     HMTNTRITDV EIMEKRYPVI VKEFSVRYGS GGDGKFKGGD GVVREIQFLK NFTVSILSER
     RSLQPRGLMG GENAERGLNL VLKNNGKYIN IGSKNSINIE RNESIIIFTP GGGGFGQKDS
     MITDN