ID A0A0H4IZT2_9PROT Unreviewed; 447 AA.
AC A0A0H4IZT2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=VI33_04835 {ECO:0000313|EMBL:AKO66486.1};
OS Methylophilales bacterium MBRS-H7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OM43 clade.
OX NCBI_TaxID=1623450 {ECO:0000313|EMBL:AKO66486.1, ECO:0000313|Proteomes:UP000066549};
RN [1] {ECO:0000313|EMBL:AKO66486.1, ECO:0000313|Proteomes:UP000066549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBRSH7 {ECO:0000313|EMBL:AKO66486.1,
RC ECO:0000313|Proteomes:UP000066549};
RA Jimenez-Infante F., Ngugi D.K., Vinu M., Alam I., Kamau A., Blom J.,
RA Bajic V.B., Stingl U.;
RT "Comparative analysis of the OM43 clade including a novel species from Red
RT Sea uncovers genomic and metabolic diversity among marine methylotrophs.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP011002; AKO66486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4IZT2; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000066549; 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:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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; 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; PF00583; Acetyltransf_1; 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}; Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01105};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01105};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105};
KW Reference proteome {ECO:0000313|Proteomes:UP000066549};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01105}.
FT DOMAIN 302..431
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 447 AA; 50962 MW; 68252C5C61217854 CRC64;
MDNLVGQSSV DFISAFRSAA PYIHHYRNKI FVIAFDGFAL ESISFVNLCT DINLLHSLGI
KIILIHGIRP FIDLRLDKNN IKSRFHKHQR ITTAEMMPHI IEANGLVKTK IEAALSSNIY
HNNIFKSELK ISSGNFLMAK PRGVIDGVDM EQTGVIREIN HEAIIEKLNH NEIVIMSPIG
YSPIGEIFNL SFESSASKIA SSIKAEKLIY ITENNGVQNI RGEFISEMTS IKLNNLISHI
KESEHPEFIE KNTLPILEGA AQGLREGLAK IHLVNRHING SLIMELFTNQ GQGTVITTEK
IEKFRSADIQ DAKVIEKMIN PLIKTQIIAD RSLEKIEMEI QHFHILEFDN KILGCAQVKH
YDGISEIACF AINENYQNMG YGKKLLEYCE NECKKVNNKT FIMTTQSSHW FMENDFKQGN
INDLPDEKKR EYSLQRNSKI FLKELEQ
//
