ID   ARG56_NEUCR             Reviewed;         871 AA.
AC   P54898; Q7RVL1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 68.
DE   RecName: Full=Protein arg-6, mitochondrial;
DE   Contains:
DE     RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase;
DE              EC=1.2.1.38;
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;
DE     AltName: Full=NAG kinase;
DE              Short=AGK;
DE     AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase;
DE   Flags: Precursor;
GN   Name=arg-6; ORFNames=NCU00567;
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=5141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 45-62 AND
RP   532-569.
RC   STRAIN=NCN53 / FGSC 7595;
RX   MEDLINE=94179195; PubMed=7907589;
RA   Gessert S.F., Kim J.H., Nargang F.E., Weiss R.L.;
RT   "A polyprotein precursor of two mitochondrial enzymes in Neurospora
RT   crassa. Gene structure and precursor processing.";
RL   J. Biol. Chem. 269:8189-8203(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   MEDLINE=22598136; PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA   Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+)
CC       + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
CC   -!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-
CC       glutamate 5-phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 2/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 3/4.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- PTM: The protein precursor is cleaved into the two biologically
CC       active enzymes, the kinase and the reductase.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       acetylglutamate kinase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC       dehydrogenase family.
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DR   EMBL; L27746; AAB05636.1; -; Genomic_DNA.
DR   EMBL; AABX02000002; EAA35492.1; -; Genomic_DNA.
DR   PIR; A53429; A53429.
DR   HSSP; P11445; 1GSJ.
DR   BRENDA; 1.2.1.38; 266.
DR   BRENDA; 2.7.2.8; 266.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase...; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR004662; AcgluKinase.
DR   InterPro; IPR000706; AGPR_act_site.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR006855; DUF619.
DR   InterPro; IPR011241; NAGK_NAGSA.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_C.
DR   Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF04768; DUF619; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   PIRSF; PIRSF036440; ARG5-6; 1.
DR   ProDom; PD003765; AGPR_act_site; 1.
DR   TIGRFAMs; TIGR00761; argB; 1.
DR   TIGRFAMs; TIGR01850; argC; 1.
DR   PROSITE; PS01224; ARGC; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Direct protein sequencing; Kinase; Mitochondrion;
KW   Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase;
KW   Transferase; Transit peptide.
FT   TRANSIT       1     44       Mitochondrion.
FT   CHAIN        45    531       Acetylglutamate kinase.
FT                                /FTId=PRO_0000002069.
FT   CHAIN       532    871       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_0000002070.
FT   ACT_SITE    689    689       By similarity.
FT   CONFLICT     11     11       G -> A (in Ref. 2; EAA35492).
SQ   SEQUENCE   871 AA;  95889 MW;  C2C44CD9CD1EB454 CRC64;
     MYSACAVALR GGARRVVRRV PKSARALPRA AAARRQISTT AARSTDLTTR GMIVQTLSSV
     GSKREVQQYL SLFTSVSSQR FAVIKVGGAI LTDYLDELCA ALKFLYTVGL YPVIVHGAGP
     QLNRLLEDAG VEPQFEEGIR VTDAKTLRVA RDLFLQENLK LVNKLEEMGV HAQPLTTGMF
     RADYLNKEKW GLVGKVTGVN KQAIETAISN GYLPILTSMA ETDDGQILNV NADVAAAELA
     RALEPLKVVY LSEKGGLFDA GGQKISAINL DEEYEHLMSQ AWVKYGTRLK IKEIKELLDT
     LPRTTSVAII HPEELQKELF TDSGAGTLIR RGSKLQASTS LSEFKDLEAL KSVLIRDREG
     PDAKETVEKY LDFLKENPFK AYFDSSMNAL AIVLPASEGR QATLATLTIT KSGWLTNIAD
     NIFTALKKEH PSLVWTVKED DENLGWFFDK ADGSITRQGD VMFWYGIENG DEIVKLMKDF
     TENGRAMLGN SNLESRLRQA ASKPAAQQVR GYSTLARRPA LPKFSISNRR GYLTQTNPNP
     PVGKQNASMD RPARVALIGA RGYTGQELIR LIDSHPNMEL HHVSSRELAG KKLEGYNKQE
     VIYENLSPED VRDMEKRGEI DCWVMALPNG VCKPFVEAVW EGRKASGHKS VIIDLSADYR
     FDNKWTYGLP ELVQRSNIIQ ATQIANPGCY ATAAQLGISP LVPHLGGMPH VFGVSGYSGA
     GTKPSPKNDV ENLTNNIIPY SLTGHIHERE VSSQLGAEIA FMPHVAVWFR GIHHTISIPL
     NKSMTSRDIR QLYQDRYAGE KLVKVVGEAP SVKNIGGKHG VEIGGFEVDK SGRRVVICAT
     IDNLLKGAAT QCLQNMNLAL GYAEYEGIPT M
//