(data stored in ACNUC7421 zone)

SWISSPROT: A8FQ78_SHESH

ID   A8FQ78_SHESH            Unreviewed;       439 AA.
AC   A8FQ78;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 69.
DE   RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01105};
DE            EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_01105};
DE   AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_01105};
DE            Short=AGS {ECO:0000256|HAMAP-Rule:MF_01105};
DE            Short=NAGS {ECO:0000256|HAMAP-Rule:MF_01105};
GN   Name=argA {ECO:0000256|HAMAP-Rule:MF_01105};
GN   OrderedLocusNames=Ssed_0388 {ECO:0000313|EMBL:ABV35001.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35001.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35001.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35001.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-
CC       glutamate. {ECO:0000256|HAMAP-Rule:MF_01105,
CC       ECO:0000256|SAAS:SAAS00710226}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 1/4. {ECO:0000256|HAMAP-
CC       Rule:MF_01105, ECO:0000256|SAAS:SAAS00710223}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105}.
CC   -!- MISCELLANEOUS: In bacteria which possess the bifunctional enzyme
CC       ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ),
CC       ArgA fulfills an anaplerotic role. {ECO:0000256|HAMAP-
CC       Rule:MF_01105}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01105,
CC       ECO:0000256|SAAS:SAAS00710235}.
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DR   EMBL; CP000821; ABV35001.1; -; Genomic_DNA.
DR   RefSeq; WP_012140738.1; NC_009831.1.
DR   ProteinModelPortal; A8FQ78; -.
DR   STRING; 425104.Ssed_0388; -.
DR   EnsemblBacteria; ABV35001; ABV35001; Ssed_0388.
DR   KEGG; sse:Ssed_0388; -.
DR   eggNOG; ENOG4108DQ3; Bacteria.
DR   eggNOG; COG0548; LUCA.
DR   eggNOG; COG1246; LUCA.
DR   HOGENOM; HOG000262225; -.
DR   KO; K14682; -.
DR   OMA; KRKYNWD; -.
DR   OrthoDB; POG091H063W; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd04237; AAK_NAGS-ABP; 1.
DR   HAMAP; MF_01105; N_acetyl_glu_synth; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR033719; NAGS_kin.
DR   InterPro; IPR010167; NH2A_AcTrfase.
DR   PANTHER; PTHR30602; PTHR30602; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   PIRSF; PIRSF000423; ArgA; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR01890; N-Ac-Glu-synth; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQ78.
DR   SWISS-2DPAGE; A8FQ78.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01105,
KW   ECO:0000256|SAAS:SAAS00710233};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01105,
KW   ECO:0000256|SAAS:SAAS00828941};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01105,
KW   ECO:0000256|SAAS:SAAS00828938};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01105,
KW   ECO:0000256|SAAS:SAAS00828937, ECO:0000313|EMBL:ABV35001.1}.
FT   DOMAIN      293    432       N-acetyltransferase.
FT                                {ECO:0000259|PROSITE:PS51186}.
SQ   SEQUENCE   439 AA;  48451 MW;  95DEAC43EB8A6A99 CRC64;
     MRTTELVDGF RHSASYVNSH RGKTFVVMLG GEALAQNQFR SIINDIALLH SLGIKIVLVH
     GARPQIDEAL ADKCIVPEYY NGVRITEEDA FKVIKQVVGG LQLDITARLS MSLSNTPMQG
     AQINVVSGNF VIAQPLGVDD GVDYCLSGKV RRIDVQGLKA QLGNNGIVLL GPIAASVTGE
     SFNLTAEEVA TQIAVKLKAD KMIGFSSQKG ILDSFGEVLA ELMPNEAQQI LNNLNQESHV
     CLGTKAFLKA SIDACRNGVS RCHFVSYLDD GSLLQELFSR DGVGTQIVTE SAERLRRAGI
     GDIGGILDLI RPLEEKGILV RRSREQLEME IEQFMLIERD SLVIGCAAFY PFEEDNAGEF
     ACLVVHPEYR DADRGSILLN NIIGQARVRG YSRLFALTTR SIHWFLEHGF EIVEVDELPD
     KKKQLYNYQR KSKILALEL
//

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