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UniProtKB/Swiss-Prot entry P54898


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARG56_NEUCR
Primary accession number P54898
Secondary accession number Q7RVL1
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 64)
Name and origin of the protein
Protein name Protein arg-6, mitochondrial [Precursor]
Synonyms None
Contains N-acetyl-gamma-glutamyl-phosphate reductase
     (EC 1.2.1.38)
     (N-acetyl-glutamate semialdehyde dehydrogenase)
     (NAGSA dehydrogenase)
Acetylglutamate kinase
     (EC 2.7.2.8)
     (NAG kinase)
     (AGK)
     (N-acetyl-L-glutamate 5-phosphotransferase)
Gene name
Name: arg-6
ORFNames: NCU00567
From
Neurospora crassa [TaxID: 5141] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 45-62 AND 532-569.
STRAIN=NCN53 / FGSC 7595;
PubMed=7907589 [NCBI, ExPASy, EBI, Israel, Japan]
Gessert S.F., Kim J.H., Nargang F.E., Weiss R.L.;
"A polyprotein precursor of two mitochondrial enzymes in Neurospora crassa. Gene structure and precursor processing.";
J. Biol. Chem. 269:8189-8203(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L27746; AAB05636.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AABX02000002; EAA35492.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A53429; A53429.
3D structure databases
HSSP P11445; 1GSJ. [HSSP ENTRY / PDB]
ModBase P54898.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from InterPro).
GO:0003991; Molecular function: acetylglutamate kinase activity (inferred from electronic annotation from InterPro).
GO:0003942; Molecular function: N-acetyl-gamma-glutamyl-phosphate reductase activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0006526; Biological process: arginine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004662; AcgluKinase.
IPR000706; AGPR_act_site.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR006855; DUF619.
IPR011241; NAGK_NAGSA.
IPR000534; Semialdehyde_DHase_NAD-bd.
IPR012280; Semialdhyde_DHase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.40.1160.10; Aa_kinase; 1.
Pfam PF00696; AA_kinase; 1.
PF04768; DUF619; 1.
PF01118; Semialdhyde_dh; 1.
PF02774; Semialdhyde_dhC; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF036440; ARG5-6; 1.
ProDom PD003765; AGPR_act_site; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00761; argB; 1.
TIGR01850; argC; 1.
PROSITE PS01224; ARGC; 1.
Other
ProtoNet P54898.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Direct protein sequencing; Kinase; Mitochondrion; Multifunctional enzyme; NADP; Oxidoreductase; Transferase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    44  44     Mitochondrion. 
CHAIN   45   531  487     Acetylglutamate kinase. PRO_0000002069
CHAIN   532   871  340     N-acetyl-gamma-glutamyl-phosphate reductase. PRO_0000002070
ACT_SITE   689   689        By similarity. 
CONFLICT   11    11        G -> A (in Ref. 2; EAA35492). 
Sequence information
Length: 871 AA [This is the length of the unprocessed precursor] Molecular weight: 95889 Da [This is the MW of the unprocessed precursor] CRC64: C2C44CD9CD1EB454 [This is a checksum on the sequence]
        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 

P54898 in FASTA format

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