Reviewed, UniProtKB/Swiss-Prot P54898 (ARG56_NEUCR)

Names and origin

Protein names

Recommended name:
    Protein arg-6, mitochondrial
Cleaved into the following 2 chains:
    1- Recommended name:
            N-acetyl-gamma-glutamyl-phosphate reductase
              EC=1.2.1.38
        Alternative name(s):
            N-acetyl-glutamate semialdehyde dehydrogenase
              Short name=NAGSA dehydrogenase
    2- Recommended name:
            Acetylglutamate kinase
              EC=2.7.2.8
        Alternative name(s):
            NAG kinase
              Short name=AGK
            N-acetyl-L-glutamate 5-phosphotransferase

Gene names

Name:	arg-6
ORF Names:	NCU00567

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	871 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular location	Mitochondrion.
Post-translational modification	The protein precursor is cleaved into the two biologically active enzymes, the kinase and the reductase.
Sequence similarities	In the N-terminal section; belongs to the acetylglutamate kinase family. In the C-terminal section; belongs to the NAGSA dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Kinase Oxidoreductase Transferase
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from electronic annotation. Source: EC NAD or NADH binding Inferred from electronic annotation. Source: InterPro acetylglutamate kinase activity Inferred from electronic annotation. Source: EC protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 44	44	Mitochondrion Ref.1
	Chain	45 – 531	487	Acetylglutamate kinase		PRO_0000002069
	Chain	532 – 871	340	N-acetyl-gamma-glutamyl-phosphate reductase		PRO_0000002070
Sites
	Active site	689	1	By similarity
Experimental info
	Sequence conflict	11	1	G → A in EAA35492. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P54898-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: C2C44CD9CD1EB454	FASTA	871	95,889
	10 20 30 40 50 60 MYSACAVALR GGARRVVRRV PKSARALPRA AAARRQISTT AARSTDLTTR GMIVQTLSSV 70 80 90 100 110 120 GSKREVQQYL SLFTSVSSQR FAVIKVGGAI LTDYLDELCA ALKFLYTVGL YPVIVHGAGP 130 140 150 160 170 180 QLNRLLEDAG VEPQFEEGIR VTDAKTLRVA RDLFLQENLK LVNKLEEMGV HAQPLTTGMF 190 200 210 220 230 240 RADYLNKEKW GLVGKVTGVN KQAIETAISN GYLPILTSMA ETDDGQILNV NADVAAAELA 250 260 270 280 290 300 RALEPLKVVY LSEKGGLFDA GGQKISAINL DEEYEHLMSQ AWVKYGTRLK IKEIKELLDT 310 320 330 340 350 360 LPRTTSVAII HPEELQKELF TDSGAGTLIR RGSKLQASTS LSEFKDLEAL KSVLIRDREG 370 380 390 400 410 420 PDAKETVEKY LDFLKENPFK AYFDSSMNAL AIVLPASEGR QATLATLTIT KSGWLTNIAD 430 440 450 460 470 480 NIFTALKKEH PSLVWTVKED DENLGWFFDK ADGSITRQGD VMFWYGIENG DEIVKLMKDF 490 500 510 520 530 540 TENGRAMLGN SNLESRLRQA ASKPAAQQVR GYSTLARRPA LPKFSISNRR GYLTQTNPNP 550 560 570 580 590 600 PVGKQNASMD RPARVALIGA RGYTGQELIR LIDSHPNMEL HHVSSRELAG KKLEGYNKQE 610 620 630 640 650 660 VIYENLSPED VRDMEKRGEI DCWVMALPNG VCKPFVEAVW EGRKASGHKS VIIDLSADYR 670 680 690 700 710 720 FDNKWTYGLP ELVQRSNIIQ ATQIANPGCY ATAAQLGISP LVPHLGGMPH VFGVSGYSGA 730 740 750 760 770 780 GTKPSPKNDV ENLTNNIIPY SLTGHIHERE VSSQLGAEIA FMPHVAVWFR GIHHTISIPL 790 800 810 820 830 840 NKSMTSRDIR QLYQDRYAGE KLVKVVGEAP SVKNIGGKHG VEIGGFEVDK SGRRVVICAT 850 860 870 IDNLLKGAAT QCLQNMNLAL GYAEYEGIPT M

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A polyprotein precursor of two mitochondrial enzymes in Neurospora crassa. Gene structure and precursor processing." Gessert S.F., Kim J.H., Nargang F.E., Weiss R.L. J. Biol. Chem. 269:8189-8203(1994) [PubMed: 7907589] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 45-62 AND 532-569. Strain: NCN53 / FGSC 7595.
[2]	"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L27746 Genomic DNA. Translation: AAB05636.1. AABX02000002 Genomic DNA. Translation: EAA35492.1.
PIR	A53429.
3D structure databases
HSSP	HSSP built from PDB template 1GSJ based on UniProtKB P11445.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.1.38. 266. 2.7.2.8. 266.
Family and domain databases
InterPro	IPR004662. AcgluKinase. IPR000706. AGPR_act_site. IPR001048. Asp/Glu/Uridylate_kinase. IPR006855. DUF619. IPR011241. NAGK_NAGSA. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_C. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
Pfam	PF00696. AA_kinase. 1 hit. PF04768. DUF619. 1 hit. PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
PIRSF	PIRSF036440. ARG5-6. 1 hit.
ProDom	PD003765. AGPR_act_site. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00761. argB. 1 hit. TIGR01850. argC. 1 hit.
PROSITE	PS01224. ARGC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARG56_NEUCR

Accession

Primary (citable) accession number: P54898
Secondary accession number(s): Q7RVL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)