ID G2FJ04_9GAMM Unreviewed; 444 AA.
AC G2FJ04;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 ECO:0000313|EMBL:EGW53206.1};
GN ORFNames=TevJSym_bi00100 {ECO:0000313|EMBL:EGW53206.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW53206.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW53206.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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:0000256|ARBA:ARBA00000016, ECO:0000256|HAMAP-
CC Rule:MF_01105};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000256|ARBA:ARBA00004925,
CC ECO:0000256|HAMAP-Rule:MF_01105}.
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), ArgA
CC fulfills an anaplerotic role. {ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC {ECO:0000256|ARBA:ARBA00009145, ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGW53206.1}.
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DR EMBL; AFZB01000035; EGW53206.1; -; Genomic_DNA.
DR RefSeq; WP_005964157.1; NZ_AFZB01000035.1.
DR AlphaFoldDB; G2FJ04; -.
DR PATRIC; fig|1049564.3.peg.2885; -.
DR eggNOG; COG0548; Bacteria.
DR eggNOG; COG1246; Bacteria.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000005167; Unassembled WGS sequence.
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 CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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 NCBIfam; TIGR01890; N-Ac-Glu-synth; 1.
DR PANTHER; PTHR30602; AMINO-ACID ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR30602:SF12; AMINO-ACID ACETYLTRANSFERASE NAGS1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF13508; Acetyltransf_7; 1.
DR PIRSF; PIRSF000423; ArgA; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01105};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01105};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_01105}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105};
KW Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01105}.
FT DOMAIN 295..442
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 444 AA; 48258 MW; C3098CB662C06015 CRC64;
MAERSPQSDP FIAWFRGSSP YIHAHRGRTF VISFGGEAVA SSGFADLIHD IALLHGLGIR
LVLVHGARPQ IEQRLQAQGT QLHYINGLRV TDDAALTCVK EAAGTVRVEI EALLSMGLAN
SPMAGARICA ASGNFVTARP IGVRDGVDYC HTGEVRRVDA EAIQQRLNSG AIAIVPPIGY
SPTGEVFNLS AADVAASVAI ALGADKLISL VEGQGLSDTD GRAITHAIPR QIDTLLAQQG
PLAEDLCQHL RGAVSACRSG VKRIHLLERQ LDGALLKELF TRDGVGTLIT AKPYETTRTA
QIDDVGGLLE LIEPLEANGT LVRRSRELLE TEIDHFTVME RDGMIVACAA LYPYPKESMA
ELACVVVHPD YRDGGRGDRL LEQMEKMAAA QNIHQLFILT TRTAHWFRER GFEAAEIQTL
PMQRQALYNY QRNAKVFIKP LTGC
//
