(data stored in SCRATCH zone)

SWISSPROT: Q2INI4_ANADE

ID   Q2INI4_ANADE            Unreviewed;       698 AA.
AC   Q2INI4;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 120.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000256|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.35 {ECO:0000256|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              Short=OATase {ECO:0000256|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine transacetylase {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_01106};
DE     AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              Short=AGSase {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Acetylglutamate kinase {ECO:0000256|HAMAP-Rule:MF_00082};
DE              EC=2.7.2.8 {ECO:0000256|HAMAP-Rule:MF_00082};
DE     AltName: Full=NAG kinase {ECO:0000256|HAMAP-Rule:MF_00082};
DE              Short=NAGK {ECO:0000256|HAMAP-Rule:MF_00082};
DE     AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00082};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000256|HAMAP-Rule:MF_01106};
GN   Name=argJ {ECO:0000256|HAMAP-Rule:MF_01106};
GN   Synonyms=argB {ECO:0000256|HAMAP-Rule:MF_00082};
GN   OrderedLocusNames=Adeh_0587 {ECO:0000313|EMBL:ABC80363.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80363.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC80363.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC80363.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-
CC       L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082,
CC       ECO:0000256|SAAS:SAAS01159244}.
CC   -!- FUNCTION: Catalyzes two activities which are involved in the
CC       cyclic version of arginine biosynthesis: the synthesis of N-
CC       acetylglutamate from glutamate and acetyl-CoA as the acetyl donor,
CC       and of ornithine by transacetylation between N(2)-acetylornithine
CC       and glutamate. {ECO:0000256|HAMAP-Rule:MF_01106}.
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;
CC         EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082,
CC         ECO:0000256|SAAS:SAAS01124576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-
CC         acetyl-L-glutamate; Xref=Rhea:RHEA:15349, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:46911, ChEBI:CHEBI:57805;
CC         EC=2.3.1.35; Evidence={ECO:0000256|HAMAP-Rule:MF_01106};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-
CC         glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.1.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01106};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 2/4. {ECO:0000256|HAMAP-
CC       Rule:MF_00082, ECO:0000256|SAAS:SAAS01090818}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC       {ECO:0000256|HAMAP-Rule:MF_01106}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106,
CC       ECO:0000256|SAAS:SAAS01159235}.
CC   -!- MISCELLANEOUS: Some bacteria possess a monofunctional ArgJ, i.e.,
CC       capable of catalyzing only the fifth step of the arginine
CC       biosynthetic pathway. {ECO:0000256|HAMAP-Rule:MF_01106}.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|HAMAP-
CC       Rule:MF_01106}.
CC   -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00082,
CC       ECO:0000256|SAAS:SAAS01076971}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00082}.
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DR   EMBL; CP000251; ABC80363.1; -; Genomic_DNA.
DR   RefSeq; WP_011419646.1; NC_007760.1.
DR   STRING; 290397.Adeh_0587; -.
DR   EnsemblBacteria; ABC80363; ABC80363; Adeh_0587.
DR   KEGG; ade:Adeh_0587; -.
DR   eggNOG; ENOG4105C5V; Bacteria.
DR   eggNOG; COG0548; LUCA.
DR   eggNOG; COG1364; LUCA.
DR   HOGENOM; HOG000002741; -.
DR   KO; K00620; -.
DR   KO; K00930; -.
DR   OMA; PKMAARE; -.
DR   BioCyc; ADEH290397:G1G5W-603-MONOMER; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
DR   CDD; cd04250; AAK_NAGK-C; 1.
DR   CDD; cd02152; OAT; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   Gene3D; 3.60.70.12; -; 1.
DR   HAMAP; MF_00082; ArgB; 1.
DR   HAMAP; MF_01106; ArgJ; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR004662; AcgluKinase_fam.
DR   InterPro; IPR002813; Arg_biosynth_ArgJ.
DR   InterPro; IPR037528; ArgB.
DR   InterPro; IPR016117; ArgJ-like_dom_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001057; Glu/AcGlu_kinase.
DR   InterPro; IPR041727; NAGK-C.
DR   PANTHER; PTHR23100; PTHR23100; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01960; ArgJ; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   SUPFAM; SSF56266; SSF56266; 1.
DR   TIGRFAMs; TIGR00761; argB; 1.
DR   TIGRFAMs; TIGR00120; ArgJ; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2INI4.
DR   SWISS-2DPAGE; Q2INI4.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01106,
KW   ECO:0000313|EMBL:ABC80363.1};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106,
KW   ECO:0000256|SAAS:SAAS01090837};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106,
KW   ECO:0000256|SAAS:SAAS01090853};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00088659};
KW   Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106,
KW   ECO:0000256|SAAS:SAAS01159248};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00461199};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00461200};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01106,
KW   ECO:0000256|SAAS:SAAS00461129, ECO:0000313|EMBL:ABC80363.1}.
FT   DOMAIN      437    674       AA_kinase. {ECO:0000259|Pfam:PF00696}.
FT   REGION      476    477       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00082}.
FT   COILED      241    261       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    178    178       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     167    167       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     178    178       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     264    264       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     390    390       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     395    395       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     498    498       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00082}.
FT   SITE        105    105       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000256|HAMAP-
FT                                Rule:MF_01106}.
FT   SITE        106    106       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000256|HAMAP-
FT                                Rule:MF_01106}.
FT   SITE        177    178       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01106}.
FT   SITE        441    441       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00082}.
FT   SITE        656    656       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00082}.
SQ   SEQUENCE   698 AA;  72912 MW;  68F5FCA4F0F491AD CRC64;
     MRIPKGFRFG GVACGLKPQR RDLALVVSDH PAAAAGLFTI NKAAAAPVLD ARTRVPAEGI
     RAIVVNSGNA NALTGPAGLD DVTVIRSAVA DALGIQKRAV LTASTGVIGA RLPAMKVVTA
     MPALVDQLGD HPDLAAEAIM TTDTRPKMAA REVTLGGKTA IVTAICKGSG MLAPQLATTI
     CLLVTDAAVT PRALQDALAR AVHRTLEMVT VDGEMSTNDT VYALANGLAG NPRISDPGPD
     LDRLETALSD LLEEMARAMA ADGEGATKLV EVVVSGAPSD EAARDCARAV ASSPLVKAAL
     FGADPNWGRV LATVGARAGA MSYPIDPYRA RVVLQGVTVF EGGAPVELDR EMLRTRMRDS
     RIDVLVELAD GAARAVAWGC DLSYDYVKIN ADYTSLIVQR PDGGVGKDDR VSNYSPAFKR
     TLLAEALKYI AAFSGQVAVI KYGGAAMVKD SLKAAFAEDV TLLKKVGLKP VVVHGGAPEI
     TRTLEKLGER SEFVDGMRIT DAQSLPVVEM VLTGKVNQEL VALLNARSAG AVGLSGKDGQ
     LLRARKAVHE SGRDLGYVGE VVEVNTKFLR MFLDGGYVPV ISPIGLTEEG TGLSINADDV
     AAAIAVALGA PKLIYLTDVP GVLESAPDGQ LVRQLTLADL DRRIQAGAIT GGMKWKAWAI
     QTALRGGVGR VHVLDGRQPH TVIAELFTDR GVGSLVTA
//

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