(data stored in SCRATCH zone)

SWISSPROT: Q6BLU1_DEBHA

ID   Q6BLU1_DEBHA            Unreviewed;       849 AA.
AC   Q6BLU1;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 102.
DE   SubName: Full=DEHA2F10736p {ECO:0000313|EMBL:CAG89175.2};
GN   OrderedLocusNames=DEHA2F10736g {ECO:0000313|EMBL:CAG89175.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89175.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89175.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 2/4.
CC       {ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 3/4.
CC       {ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion
CC       {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
CC       acetylglutamate kinase family. {ECO:0000256|PIRNR:PIRNR036440}.
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DR   EMBL; CR382138; CAG89175.2; -; Genomic_DNA.
DR   RefSeq; XP_460830.2; XM_460830.1.
DR   STRING; 4959.XP_460830.2; -.
DR   EnsemblFungi; CAG89175; CAG89175; DEHA2F10736g.
DR   GeneID; 2904346; -.
DR   KEGG; dha:DEHA2F10736g; -.
DR   HOGENOM; HOG000201928; -.
DR   InParanoid; Q6BLU1; -.
DR   KO; K12659; -.
DR   OMA; PWVKYGT; -.
DR   OrthoDB; 351612at2759; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR012280; Semialdhyde_DH_dimer_dom.
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   Pfam; PF02774; Semialdhyde_dhC; 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; Q6BLU1.
DR   SWISS-2DPAGE; Q6BLU1.
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR036440};
KW   Arginine biosynthesis {ECO:0000256|PIRNR:PIRNR036440};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR036440};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Kinase {ECO:0000256|PIRNR:PIRNR036440};
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   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transferase {ECO:0000256|PIRNR:PIRNR036440,
KW   ECO:0000256|SAAS:SAAS00239089}.
FT   DOMAIN      332    483       N-acetyltransferase.
FT                                {ECO:0000259|PROSITE:PS51731}.
FT   ACT_SITE    661    661       {ECO:0000256|PROSITE-ProRule:PRU10010}.
SQ   SEQUENCE   849 AA;  93763 MW;  6BC558B1D5A97AD1 CRC64;
     MLRQVVGRSV VKRLSSVANK EIVGSVSLSN RLRSTKTTTR FYSTRSTVVQ LLNNIGSKRE
     VEQYLKYFTS VSQQQFAVIK VGGAIITQQL PELASCLAFL YHVGLYPIVL HGTGPQINEL
     LENEGVEPEY SDGIRITNPK TMEVVRKCFL EQNLRLVTAL EKMGVHARPI TAGVFGADYL
     DKDKYQLVGK VNSVNKSPVE SAIEAGYLPI LTSLAETPSG QLLNVNADVA AGELAREFEP
     LKIVYLNEKG GIINGNTGEK VSMINLDEEY DDLMKESWVK YGTKLKIKEI HDLLQHLPRS
     SSVAIIDVDD LQKELFTDSG AGTLIRRGYK LISRNSLKEF GNPDLLRAAL LRDPEIKSGK
     LSVASYLKHL ESIEFKSYGD EPLEVLAIVT KNGSRFPKLD KFLSSRTGWL NNVTDNIFNS
     IKKDYKSLYW IVSENDSNLS WYFSKSDGSF SKNGEILFWY GLNTEEVSQL INQFDSSSIG
     SALSSSSESG IFSSPTQKKG LHTMARRSYS SNPNPPIREG KNTQKAKVAL IGARGYTGQN
     LINMIDSHPF LELSHVSSRE LKGQKLKGYN KDNIVYSNLQ VEDIKELEKN NEVDVWVMAL
     PNGVCKPFVE AIESIPNNKS KIIDLSADYR FDTTGEWVYG LPELNDRNAI ASAKKISNPG
     CYATAAQCAI APLVSYINGT PSIFGVSGYS GAGTKPSPKN DVKFLANNII PYSLTDHIHE
     KEISSQLGLD VAFTPHVAQW FQGISHTISI PIKPKSLSSR EIRNIYQDRY QGEQLITISG
     EAPLVKDISG KHGVVVGGFA VNSKQDRVVI VATIDNLLKG ASTQCLQNIN LTMGYGEFEG
     IPDDLVIRG
//

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