ARG56_NEUCR
ID ARG56_NEUCR Reviewed; 871 AA.
AC P54898; Q7RVL1; V5IRF5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 144.
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=N-acetyl-L-glutamate 5-phosphotransferase;
DE AltName: Full=NAG kinase;
DE Short=AGK;
DE Flags: Precursor;
GN Name=arg-6; Synonyms=orn-2; ORFNames=NCU00567;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 45-62 AND
RP 532-569.
RC STRAIN=NCN53 / FGSC 7595;
RX PubMed=7907589; DOI=10.1016/s0021-9258(17)37179-x;
RA Gessert S.F., Kim J.H., Nargang F.E., Weiss R.L.;
RT "A polyprotein precursor of two mitochondrial enzymes in Neurospora crassa.
RT 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 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., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., 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., Paulsen I.,
RA 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:
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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- PTM: The protein precursor is cleaved into the two biologically active
CC enzymes, the kinase and the reductase.
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; L27746; AAB05636.1; -; Genomic_DNA.
DR EMBL; CM002236; ESA44319.1; -; Genomic_DNA.
DR EMBL; CM002236; ESA44320.1; -; Genomic_DNA.
DR PIR; A53429; A53429.
DR RefSeq; XP_011392782.1; XM_011394480.1.
DR RefSeq; XP_011392783.1; XM_011394481.1.
DR AlphaFoldDB; P54898; -.
DR SMR; P54898; -.
DR STRING; 5141.EFNCRP00000000910; -.
DR PRIDE; P54898; -.
DR EnsemblFungi; ESA44319; ESA44319; NCU00567.
DR EnsemblFungi; ESA44320; ESA44320; NCU00567.
DR GeneID; 3880877; -.
DR KEGG; ncr:NCU00567; -.
DR VEuPathDB; FungiDB:NCU00567; -.
DR HOGENOM; CLU_006384_4_0_1; -.
DR InParanoid; P54898; -.
DR UniPathway; UPA00068; UER00107.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:EnsemblFungi.
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 Direct protein sequencing; Kinase; Mitochondrion; Multifunctional enzyme;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7907589"
FT CHAIN 45..531
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000002069"
FT CHAIN 532..871
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000002070"
FT DOMAIN 336..488
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 689
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10010"
FT CONFLICT 11
FT /note="A -> G (in Ref. 1; AAB05636)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 871 AA; 95903 MW; 1FFD2E794F740660 CRC64;
MYSACAVALR AGARRVVRRV 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
