(data stored in SCRATCH zone)

SWISSPROT: Q4WCZ1_ASPFU

ID   Q4WCZ1_ASPFU            Unreviewed;       906 AA.
AC   Q4WCZ1;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 102.
DE   SubName: Full=Acetylglutamate kinase, putative {ECO:0000313|EMBL:EAL85747.1};
DE            EC=1.2.1.38 {ECO:0000313|EMBL:EAL85747.1};
GN   ORFNames=AFUA_6G02910 {ECO:0000313|EMBL:EAL85747.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL85747.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85747.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 2/4.
CC       {ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 3/4.
CC       {ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC       kinase family. {ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL85747.1}.
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DR   EMBL; AAHF01000012; EAL85747.1; -; Genomic_DNA.
DR   RefSeq; XP_747785.1; XM_742692.1.
DR   STRING; 746128.CADAFUBP00009270; -.
DR   PRIDE; Q4WCZ1; -.
DR   EnsemblFungi; EAL85747; EAL85747; AFUA_6G02910.
DR   GeneID; 3505140; -.
DR   KEGG; afm:AFUA_6G02910; -.
DR   EuPathDB; FungiDB:Afu6g02910; -.
DR   HOGENOM; HOG000201928; -.
DR   InParanoid; Q4WCZ1; -.
DR   KO; K12659; -.
DR   OMA; TSRDIRN; -.
DR   OrthoDB; 351612at2759; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0034618; F:arginine binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; 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:UniProtKB-UniRule.
DR   GO; GO:0006526; P:arginine biosynthetic process; IMP:AspGD.
DR   GO; GO:1900706; P:positive regulation of siderophore biosynthetic process; IMP:AspGD.
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   3: Inferred from homology;
DR   PRODOM; Q4WCZ1.
DR   SWISS-2DPAGE; Q4WCZ1.
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR036440};
KW   Arginine biosynthesis {ECO:0000256|PIRNR:PIRNR036440};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR036440};
KW   Kinase {ECO:0000256|PIRNR:PIRNR036440, ECO:0000313|EMBL:EAL85747.1};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR036440};
KW   Multifunctional enzyme {ECO:0000256|PIRNR:PIRNR036440};
KW   NADP {ECO:0000256|PIRNR:PIRNR036440};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR036440};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR036440,
KW   ECO:0000313|EMBL:EAL85747.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000256|PIRNR:PIRNR036440, ECO:0000256|SAAS:SAAS00239089}.
FT   DOMAIN          355..510
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51731"
FT   REGION          567..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        724
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   906 AA;  99446 MW;  5E26A372F49363E1 CRC64;
     MLVDKMFSLR TTVRRASTSK PLRALSAPHA VSSARLSSPR HALKASAVPL LQSRSYSRAA
     DPHLSSTRST VVQLLSNIGS KREVQQYLSH FTSVSSQQFA VIKVGGAIIT EHLQTLSSAL
     AFLNHVGLYP IVVHGAGPQL NRMLEAAGVE PHFEDGIRVT DGKTLALARK LFLEENLKLI
     EELERMGVRA RPINAGVFYA DYLDKEKYNL VGKINGVNKK PIESAIEAGC LPILTSMAET
     PDGQVLNVNA DVAAGELARA LQPLKIVYLA EKGGLFNGDT GEKISVINLD EEYDHLMTQW
     WVRHGTRLKI KEMKELLNDL PRTSSVAIIH PADLQKELFT DSGAGTLIRR GNKVHTKTSL
     SEFEDLEKLK DVLVRDREGL DARATVDRYV EGLKERDFKV YYDEPMEALA VVLPPSKDNS
     SSFPHLATFT ITKSGWLSNV ADNVFAAIKK DFPQLVWTVK ENDENLTWFF DKADGSLSRD
     GEVLFWYGIE SGEEVKQLVQ EFNQHGRQMF GDINLEARLQ RAAQAATNIG KGFGASGASV
     EQKRAFSSTA NALRAARFGR PAVSPRVVRS YSTTNPNPPL GEKNMSNNRP SKVALIGARG
     YTGQALINLL NAHPYMDLRH VSSRELAGKK LQGYDKREII YENLSPEDVK RMSANGDVDC
     WVMALPNGVC KPFVDAVDQG SETGNVIVDL SADYRFDDKW TYGLPELVNR GKIAQATRIS
     NPGCYATAAQ IGIAPLVPYL GGQPTVFGVS GYSGAGTKPS PKNDVQNLTN NIIPYSLTDH
     IHEREISAQL GTSIAFIPHV AVWFQGIHHT ISIPLNQEMT SRDIRNIYQE RYAGEKLVKI
     IGEAPLVKNI AGRHGIEVGG FAVHSSGKRV VVCATIDNLL KGAATQCLQN MNLALGYGEY
     EGIPLE
//

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