ID   ARG56_SCHPO             Reviewed;         885 AA.
AC   P31318;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=Protein arg11, mitochondrial;
DE   Contains:
DE     RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase;
DE              EC=1.2.1.38 {ECO:0000269|PubMed:1313366};
DE     AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase;
DE              Short=NAGSA dehydrogenase;
DE   Contains:
DE     RecName: Full=Acetylglutamate kinase;
DE              EC=2.7.2.8 {ECO:0000269|PubMed:1313366};
DE     AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase;
DE     AltName: Full=NAG kinase;
DE              Short=AGK;
DE   Flags: Precursor;
GN   Name=arg11; ORFNames=SPAC4G9.09c;
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 [GENOMIC DNA], CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR
RP   LOCATION, AND PROTEOLYTIC PROCESSING.
RC   STRAIN=ATCC 38365 / 975;
RX   PubMed=1313366; DOI=10.1111/j.1432-1033.1992.tb16749.x;
RA   van Huffel C., Dubois E., Messenguy F.;
RT   "Cloning and sequencing of arg3 and arg11 genes of Schizosaccharomyces
RT   pombe on a 10-kb DNA fragment. Heterologous expression and mitochondrial
RT   targeting of their translation products.";
RL   Eur. J. Biochem. 205:33-43(1992).
RN   [2]
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate =
CC         H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:21588,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38;
CC         Evidence={ECO:0000269|PubMed:1313366};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-
CC         phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8;
CC         Evidence={ECO:0000269|PubMed:1313366};
CC   -!- ACTIVITY REGULATION: The kinase activity is inhibited by arginine.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 2/4. {ECO:0000305|PubMed:1313366}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 3/4. {ECO:0000305|PubMed:1313366}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:1313366}.
CC   -!- PTM: The protein precursor is probably cleaved into the two
CC       biologically active enzymes, the kinase and the reductase.
CC       {ECO:0000305|PubMed:1313366}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC       kinase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; X63576; CAA45132.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA93559.1; -; Genomic_DNA.
DR   PIR; S22389; S22389.
DR   RefSeq; NP_593691.1; NM_001019123.2.
DR   AlphaFoldDB; P31318; -.
DR   SMR; P31318; -.
DR   BioGRID; 279813; 47.
DR   STRING; 4896.SPAC4G9.09c.1; -.
DR   iPTMnet; P31318; -.
DR   MaxQB; P31318; -.
DR   PaxDb; P31318; -.
DR   PRIDE; P31318; -.
DR   EnsemblFungi; SPAC4G9.09c.1; SPAC4G9.09c.1:pep; SPAC4G9.09c.
DR   GeneID; 2543391; -.
DR   KEGG; spo:SPAC4G9.09c; -.
DR   PomBase; SPAC4G9.09c; arg11.
DR   VEuPathDB; FungiDB:SPAC4G9.09c; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   eggNOG; KOG4354; Eukaryota.
DR   HOGENOM; CLU_006384_4_0_1; -.
DR   InParanoid; P31318; -.
DR   OMA; VWVMALP; -.
DR   PhylomeDB; P31318; -.
DR   Reactome; R-SPO-70635; Urea cycle.
DR   UniPathway; UPA00068; UER00107.
DR   UniPathway; UPA00068; UER00108.
DR   PRO; PR:P31318; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; ISO:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IMP:PomBase.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IMP:PomBase.
DR   GO; GO:0006592; P:ornithine biosynthetic process; IC:PomBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04252; AAK_NAGK-fArgBP; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   HAMAP; MF_00150; ArgC_type1; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR004662; AcgluKinase_fam.
DR   InterPro; IPR023013; AGPR_AS.
DR   InterPro; IPR000706; AGPR_type-1.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041734; NAGK-fArgBP.
DR   InterPro; IPR011241; NAGK/NAGSA.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF04768; NAT; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   PIRSF; PIRSF036440; ARG5-6; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00761; argB; 1.
DR   TIGRFAMs; TIGR01850; argC; 1.
DR   PROSITE; PS01224; ARGC; 1.
DR   PROSITE; PS51731; GNAT_NAGS; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Cleavage on pair of basic residues; Kinase; Mitochondrion;
KW   Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..59
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           60..550
FT                   /note="Acetylglutamate kinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000002071"
FT   CHAIN           551..885
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000002072"
FT   DOMAIN          346..499
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          503..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        703
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10010"
FT   VARIANT         261
FT                   /note="V -> D (in strain: 975)"
FT   VARIANT         345
FT                   /note="G -> P (in strain: 975)"
SQ   SEQUENCE   885 AA;  97705 MW;  3AA1A5082431B118 CRC64;
     MLIELQQIVK SGLVRNGAKH CTKRSLLCSN ASVIASKRFQ GSFAPGQQQP LNPLAKPIEQ
     DRDAIIRILS SIGSRREVEQ YLRYFTSFEA QRFAIIKVGG AIITDELDTL AQSLAFLNHV
     GLYPIVVHGA GPQLNKILAS RNVEPEYSDG IRITDAETLS VARKVFLEEN AKLVDALEKL
     GTRARPITGG VFQAEYLDKE KYKYVGKIVK VNKAPIEHSI RAGTLPILTS MAETASGQLL
     NVNADITAGE LARVLKPLKV VYLNEKGGLI NGETKKKISS IYLDREYDGL MKQPWVKYGT
     KLKIKEIKEL LDTLPRTSSV AIISTKDLQK ELFTESGAGT LISRGFVINK HDSLDSIPDA
     ALENLIIQKN SLAAPSESLK QFKDTLKDRK LRIYSDSFNE SVAIVDTTDS SLPVLLAFGA
     ADNNWLNNVV DSILTTLKAD FPSLLWRLQP SAKNLEWFFS KSEGTLFANN FYYFWYGVKD
     LNKISKFIQS DKPFADAIIQ TQSTKPPTAS STTNNPSSSQ INQKRSYSTS SLFSKNKKMN
     RSLFLKGGKR FFSAEAQKTQ KPLKAVSSKP AKVVLLGARG YTGKNLIGLI NTHPYLELSH
     VSSRELEGTK LPGYTKKEIQ YVNLSTDDVK KLEEEGAVDA WVMALPNGVC KPYVDALTSA
     NGKSVIVDLS ADYRFEPSWQ YGLPELNDRE ALRNSKRISN PGCYATGSQV GLTPILSLID
     GQPSIFGVSG YSGAGTKPSP KNDLNVLTNN LIPYSLTDHI HEREISYRLK QPVAFIPHVA
     QWFQGITLTI NVPLKKSITS RELRNLYQDR YNGEPLIHVQ GDVPLVKDNA HKHHVSVGGF
     GVHSSGKRAV IVVTIDNLLK GAATQALQNL NLSCGYDEYA GIHLD