ID Q6CSP3_KLULA Unreviewed; 1286 AA. AC Q6CSP3; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 28-JAN-2026, entry version 97. DE SubName: Full=KLLA0C18975p {ECO:0000313|EMBL:CAH01897.1}; GN ORFNames=KLLA0_C18975g {ECO:0000313|EMBL:CAH01897.1}; OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=284590 {ECO:0000313|EMBL:CAH01897.1, ECO:0000313|Proteomes:UP000000598}; RN [1] {ECO:0000313|EMBL:CAH01897.1, ECO:0000313|Proteomes:UP000000598} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / RC WM37 {ECO:0000313|Proteomes:UP000000598}; RX PubMed=15229592; DOI=10.1038/nature02579; RG Genolevures; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L., RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- SIMILARITY: Belongs to the oxoprolinase family. CC {ECO:0000256|ARBA:ARBA00010403}. 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; CR382123; CAH01897.1; -; Genomic_DNA. DR FunCoup; Q6CSP3; 888. DR STRING; 284590.Q6CSP3; -. DR PaxDb; 284590-Q6CSP3; -. DR KEGG; kla:KLLA0_C18975g; -. DR eggNOG; KOG1939; Eukaryota. DR HOGENOM; CLU_002157_0_1_1; -. DR InParanoid; Q6CSP3; -. DR OMA; TDCNVML; -. DR Proteomes; UP000000598; Chromosome C. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IEA:TreeGrafter. DR GO; GO:0006749; P:glutathione metabolic process; IEA:TreeGrafter. DR InterPro; IPR049517; ACX-like_C. DR InterPro; IPR008040; Hydant_A_N. DR InterPro; IPR002821; Hydantoinase_A. DR InterPro; IPR003692; Hydantoinase_B. DR InterPro; IPR045079; Oxoprolinase-like. DR PANTHER; PTHR11365:SF2; 5-OXOPROLINASE; 1. DR PANTHER; PTHR11365; 5-OXOPROLINASE RELATED; 1. DR Pfam; PF19278; Hydant_A_C; 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 Reference proteome {ECO:0000313|Proteomes:UP000000598}. FT DOMAIN 13..228 FT /note="Hydantoinase/oxoprolinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF05378" FT DOMAIN 248..541 FT /note="Hydantoinase A/oxoprolinase" FT /evidence="ECO:0000259|Pfam:PF01968" FT DOMAIN 675..730 FT /note="Acetophenone carboxylase-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF19278" FT DOMAIN 749..1285 FT /note="Hydantoinase B/oxoprolinase" FT /evidence="ECO:0000259|Pfam:PF02538" SQ SEQUENCE 1286 AA; 140586 MW; 3480EF34F2F1929D CRC64; MTVDRSEKTG GIRIAVDRGG TFTDCIGNPG TNRQEDDVVI KLLSVDPKNY PDAPLEGIRR LLEIIEDRKI PRGTPLDVSG VKSVRMGTTL ATNCALERNG ERCAFITTLG FKDALLIGDQ TRPDIFDLNI RKSEPLYDMV VEVDERVTLE DFSEDPDNVK STENLKDNTV MGTSGEVVRV LKRPDLSSIE ATLRLVYDSG IKSIAVALLH AYTYPDHELL IGKIAHKIGF KHVSLSSQVS PMIKFLPRAH SSVADAYLTP VIKKYLESIE SGLTNAENTN VQFMQSDGGL VDGKKFSGLK SILSGPAGGV VGYSSTCYDD ENRIPLIGFD MGGTSTDVSR YGDGKLEHIF ETTTAGIVIQ SPQLDINTVA AGGSSRLFWE NGLFRVGPES ATADPGPAAY RKGGPLTITD ANLFLGRLVP EFFPSIFGPN EDETLDLETT TKLFLELTDT INKDLNANFT PDEIAYGFLK VANESMARPI RAITEAKGHA VQNHRLVTFG GAGGQHAVAV AKSLGIKEVL AHRYSSILSA YGIFLADVVE EKQEPCSFIL EDSSTMDKVK LRFDNLCAMS KASFRNQGFD DSDLVFEKYL NLRYEGTETS LMILQEDDSY EFKKWFSRCH KTEFGFDSAD KNIIVDDIRV RTIAKSNVRK EDSVDSQLSM LSRNAIDRKT HASFTKLVYF NGKRVETPVY RIEKMPLGSV ITGPAILADG TQTNVIPPNT EAVILKSHIF IKLLSAVDDA KPVSDDEIDP VLLSIFSHRF MDIAEQMGNQ LRKTSVSTNV KERLDFSCAL FDNTGNLVAN APHVPVHLGS MSTCIAAQAK LWKGKLKPGD VIITNHPEIG GTHLPDITII TPAFSEKTGE LIFYVASRAH HADIGGILPG SVPPNSKELY EEGAAIYSEL ITKDGEFQND LVKEYLLYKP AQYPKCSGSR KISDNISDLK AQVAANNKGI QLIQKLNEEY GITVIKRYME AIQDNASTTI KSMLRKMANH FNTTEFSGED LMDDGSTIKL KVNLDVENEE YTFDFEGTSP QIYGNLNAPE AITNSAILYC LRCLVGEDIP LNQGCLKPLT IKIPKGSILS PTKGMAVVGG NVLTSQRVTD VVLKTFQVMA DSQGDCNNFT FGTGGKDPIT GETKDGFGYY ETICGGHGAG CDSWRGNGWN GADAVHTNMT NTRITDVEIF ERRYPVILNE FSIRQNSGGK GKYKGGNGIV RDITFRKEVQ ASILSERRVI APHGIAGGGD GARGMNIWVR HETNSKVNMG GKNTVPIRPG DRVIIMTPGG GGCGRA //