(data stored in ACNUC7421 zone)

HOGENOM: OCHA4_1_PE1012

ID   OCHA4_1_PE1012                       STANDARD;      PRT;   413 AA.
AC   OCHA4_1_PE1012; A6WXP0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ;
DE   (OCHA4_1.PE1012).
GN   Name=argJ; OrderedLocusNames=Oant_1023;
OS   OCHROBACTRUM ANTHROPI ATCC 49188.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae;
OC   Ochrobactrum.
OX   NCBI_TaxID=439375;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS OCHA4_1.PE1012.
CC       Ochrobactrum anthropi ATCC 49188 chromosome 1, complete sequence.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:A6WXP0_OCHA4
CC   -!- FUNCTION: Catalyzes two activities which are involved in the
CC       cyclic version of arginine biosynthesis: the synthesis of
CC       acetylglutamate from glutamate and acetyl-CoA, and of ornithine by
CC       transacetylation between acetylornithine and glutamate (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-
CC       glutamate.
CC   -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L-
CC       ornithine + N-acetyl-L-glutamate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-
CC       acetyl-L-ornithine (cyclic): step 1/1.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 1/4.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: Some bacteria possess a monofunctional ArgJ, i.e.,
CC       capable of catalyzing only the fifth step of the arginine
CC       biosynthetic pathway (By similarity).
CC   -!- SIMILARITY: Belongs to the ArgJ family.
CC   -!- GENE_FAMILY: HOG000022798 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A6WXP0; -.
DR   EMBL; CP000758; ABS13744.1; -; Genomic_DNA.
DR   RefSeq; YP_001369573.1; NC_009667.1.
DR   ProteinModelPortal; A6WXP0; -.
DR   STRING; A6WXP0; -.
DR   MEROPS; T05.001; -.
DR   GeneID; 5379953; -.
DR   GenomeReviews; CP000758_GR; Oant_1023.
DR   KEGG; oan:Oant_1023; -.
DR   eggNOG; COG1364; -.
DR   OMA; FPKLATR; -.
DR   ProtClustDB; PRK05388; -.
DR   BioCyc; OANT439375:OANT_1023-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:HAMAP.
DR   GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01106; ArgJ; 1; -.
DR   InterPro; IPR002813; Arg_biosynth_ArgJ.
DR   InterPro; IPR016117; Pept_S58_DmpA/Arg_biosyn_ArgJ.
DR   PANTHER; PTHR23100; ArgJ; 1.
DR   Pfam; PF01960; ArgJ; 1.
DR   SUPFAM; SSF56266; Pept_S58_DmpA/Arg_biosyn_ArgJ; 1.
DR   TIGRFAMs; TIGR00120; ArgJ; 1.
DR   HOGENOMDNA; OCHA4_1.PE1012; -.
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Autocatalytic cleavage; Complete proteome; Cytoplasm;
KW   Multifunctional enzyme; Transferase.
SQ   SEQUENCE   413 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSASVSPLAP KHYPTMPVVH GVRIATAAAG IKYKGRTDVM LMVFDRPAEA AGVFTRSLCP
     SAPVDFCRRN LVYGKARAVV VNSGNANAFT GVKGREATEA TAEAAAKAVG CATTDVFLAS
     TGVIGEPLDA SKFAHLLGDM NKDAVEDFWT EAAKAIMTTD TYPKVATETV LLGQVPVTIN
     GIAKGAGMIA PDMATMLSFV VTDAPIKADV LQSLLSKGVG STFNAVTVDS DTSTSDTLML
     FATGAAAERG APEITDPADK RLGEFKKALG RLLKSLALQV VRDGEGARKM VEVEVTGAKS
     AASAKKIALS IANSPLVKTA VAGEDANWGR VVMAVGKAGE PADRDLLAIW FGDIRVAHQG
     ERDPAYSEAA TSTYMQGEDI RIRVDLGIGK GKATVWTCDL TKEYVAINGD YRS
//

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