ARGA_VIBPA
ID ARGA_VIBPA Reviewed; 445 AA.
AC Q87M87;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01105};
DE EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01105};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01105};
DE Short=AGS {ECO:0000255|HAMAP-Rule:MF_01105};
DE Short=NAGS {ECO:0000255|HAMAP-Rule:MF_01105};
GN Name=argA {ECO:0000255|HAMAP-Rule:MF_01105}; OrderedLocusNames=VP2371;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01105};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000255|HAMAP-
CC Rule:MF_01105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01105}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01105}.
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DR EMBL; BA000031; BAC60634.1; -; Genomic_DNA.
DR RefSeq; NP_798750.1; NC_004603.1.
DR RefSeq; WP_005482311.1; NC_004603.1.
DR PDB; 3E0K; X-ray; 2.52 A; A=298-445.
DR PDBsum; 3E0K; -.
DR AlphaFoldDB; Q87M87; -.
DR SMR; Q87M87; -.
DR STRING; 223926.28807369; -.
DR EnsemblBacteria; BAC60634; BAC60634; BAC60634.
DR GeneID; 1189884; -.
DR KEGG; vpa:VP2371; -.
DR PATRIC; fig|223926.6.peg.2275; -.
DR eggNOG; COG0548; Bacteria.
DR eggNOG; COG1246; Bacteria.
DR HOGENOM; CLU_024773_0_0_6; -.
DR OMA; KRKYNWD; -.
DR UniPathway; UPA00068; UER00106.
DR EvolutionaryTrace; Q87M87; -.
DR Proteomes; UP000002493; Chromosome 1.
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:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04237; AAK_NAGS-ABP; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR HAMAP; MF_01105; N_acetyl_glu_synth; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
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; 2.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Amino-acid biosynthesis;
KW Arginine biosynthesis; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..445
FT /note="Amino-acid acetyltransferase"
FT /id="PRO_0000186809"
FT DOMAIN 299..438
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01105"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:3E0K"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:3E0K"
FT HELIX 309..321
FT /evidence="ECO:0007829|PDB:3E0K"
FT HELIX 330..336
FT /evidence="ECO:0007829|PDB:3E0K"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:3E0K"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:3E0K"
FT STRAND 348..358
FT /evidence="ECO:0007829|PDB:3E0K"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:3E0K"
FT STRAND 363..371
FT /evidence="ECO:0007829|PDB:3E0K"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:3E0K"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:3E0K"
FT HELIX 380..393
FT /evidence="ECO:0007829|PDB:3E0K"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:3E0K"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:3E0K"
FT HELIX 408..413
FT /evidence="ECO:0007829|PDB:3E0K"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:3E0K"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:3E0K"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:3E0K"
SQ SEQUENCE 445 AA; 48753 MW; B924E581D8DFF19A CRC64;
MKIRSTALVK GFRQSTPYVN AHRGKTMVIM LGGEAVAHNN FGNIINDIAL MHSLGIKVVV
VYGARPQINQ LLEKQDLTTP YHKNIRITDE AALSVVMQAA GQLQLAITAR LSMSLNNTPM
AGTQLNVVSG NFVIAQPLGV DDGVDYCHSG RIRRIDTDAI NRTLDQGSIV LLGPIASSVT
GECFNLLSEE VATQLAIKLG ADKLIGFCSE QGVIDDNGNA VAELLPIEAE HVIKTLSENH
ASDSDYNTGT LRFLKGSIAA CRAGVPRSHL ISYKVDGALI QELFSFDGIG TQVVMASAEQ
VRQAGIDDIG GILELIHPLE EQGILVRRSR EQLEQEIGKF TIIEKDGLII GCAALYPYSE
ERKAEMACVA IHPDYRDGNR GLLLLNYMKH RSKSENINQI FVLTTHSLHW FREQGFYEVG
VDYLPGAKQG LYNFQRKSKI LALDL
