ID   PROB_SCHPO              Reviewed;         402 AA.
AC   O13810;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Probable glutamate 5-kinase;
DE            Short=GK;
DE            EC=2.7.2.11;
DE   AltName: Full=Gamma-glutamyl kinase;
GN   ORFNames=SPAC17H9.13c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to
CC       form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate;
CC         Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutamate 5-kinase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB11222.1; -; Genomic_DNA.
DR   PIR; T37879; T37879.
DR   RefSeq; NP_593583.1; NM_001019015.2.
DR   AlphaFoldDB; O13810; -.
DR   SMR; O13810; -.
DR   BioGRID; 278742; 144.
DR   STRING; 4896.SPAC17H9.13c.1; -.
DR   iPTMnet; O13810; -.
DR   MaxQB; O13810; -.
DR   PaxDb; O13810; -.
DR   PRIDE; O13810; -.
DR   EnsemblFungi; SPAC17H9.13c.1; SPAC17H9.13c.1:pep; SPAC17H9.13c.
DR   GeneID; 2542273; -.
DR   KEGG; spo:SPAC17H9.13c; -.
DR   PomBase; SPAC17H9.13c; -.
DR   VEuPathDB; FungiDB:SPAC17H9.13c; -.
DR   eggNOG; KOG1154; Eukaryota.
DR   HOGENOM; CLU_025400_1_1_1; -.
DR   InParanoid; O13810; -.
DR   OMA; TVIHRDN; -.
DR   PhylomeDB; O13810; -.
DR   UniPathway; UPA00098; UER00359.
DR   PRO; PR:O13810; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; ISO:PomBase.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; NAS:PomBase.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; EXP:PomBase.
DR   CDD; cd04242; AAK_G5K_ProB; 1.
DR   Gene3D; 2.30.130.10; -; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   HAMAP; MF_00456; ProB; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR041739; G5K_ProB.
DR   InterPro; IPR001057; Glu/AcGlu_kinase.
DR   InterPro; IPR011529; Glu_5kinase.
DR   InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR   InterPro; IPR019797; Glutamate_5-kinase_CS.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01472; PUA; 1.
DR   PIRSF; PIRSF000729; GK; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR01027; proB; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Proline biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..402
FT                   /note="Probable glutamate 5-kinase"
FT                   /id="PRO_0000109767"
FT   DOMAIN          295..373
FT                   /note="PUA"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         177..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         218..224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   402 AA;  43934 MW;  D78F550F8828B033 CRC64;
     MSPKSKSTNK TYTIVIKLGT SSICDEKTHE PLISNLSLIV ETVVKLRKLG HNVVLVSSGG
     IAMGLRRLDL PKRPSKLSAV QAIAAVGQGR LISLWDTLFT QLRQPIAQVL ITRNDIAERS
     QYVNAANTIS ELLHFGVVPI VNENDTLSVQ EIRFGDNDTL SAITAGMINA DYLFLLTDVD
     CLYTDNPRTN PDAKPILKIH DTSMVNANVS TPGSGVGTGG MKTKLIAADL GTSSGVNVII
     CRGSKPSSIF DIIRQESSDN KNESVELPLH THFVAKKQGR IRDRHFWLLH GLKSHGSLEI
     DRGAFEAITR TNRAGLLPVG VTKVHGHFSA HQAVTVIYNG EEIGRALVNY SSTEIDLIKG
     KRSKEIASIL GYNETEYVAY RDYLVVHGLN SHHDSQVSSD EH