ARGB_MYCTU
ID ARGB_MYCTU Reviewed; 294 AA.
AC P9WQ01; L0TA25; P0A4Y6; P94989;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Acetylglutamate kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE EC=2.7.2.8 {ECO:0000255|HAMAP-Rule:MF_00082};
DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00082};
DE AltName: Full=NAG kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE Short=NAGK {ECO:0000255|HAMAP-Rule:MF_00082};
GN Name=argB {ECO:0000255|HAMAP-Rule:MF_00082}; OrderedLocusNames=Rv1654;
GN ORFNames=MTCY06H11.19;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 4-294, AND SUBUNIT.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of acetylglutamate kinase from Mycobacterium
RT tuberculosis CDC1551.";
RL Submitted (AUG-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.
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; EC=2.7.2.8;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00082};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_00082}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00082}.
CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00082}.
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DR EMBL; AL123456; CCP44419.1; -; Genomic_DNA.
DR PIR; A70621; A70621.
DR RefSeq; NP_216170.1; NC_000962.3.
DR RefSeq; WP_003408161.1; NZ_NVQJ01000069.1.
DR PDB; 2AP9; X-ray; 2.80 A; A/B/C/D/E/F=4-294.
DR PDB; 7NLF; X-ray; 2.08 A; A=2-294.
DR PDB; 7NLN; X-ray; 1.92 A; A/B=2-294.
DR PDB; 7NLO; X-ray; 1.82 A; A=2-294.
DR PDB; 7NLP; X-ray; 2.21 A; A=2-294.
DR PDB; 7NLQ; X-ray; 2.50 A; A=2-294.
DR PDB; 7NLR; X-ray; 2.25 A; A=2-294.
DR PDB; 7NLS; X-ray; 2.65 A; A=2-294.
DR PDB; 7NLT; X-ray; 2.23 A; A=2-294.
DR PDB; 7NLU; X-ray; 2.23 A; A=2-294.
DR PDB; 7NLW; X-ray; 2.32 A; A=2-294.
DR PDB; 7NLX; X-ray; 2.23 A; A=2-294.
DR PDB; 7NLY; X-ray; 2.25 A; A=2-294.
DR PDB; 7NLZ; X-ray; 2.16 A; A=2-294.
DR PDB; 7NM0; X-ray; 2.28 A; A=2-294.
DR PDB; 7NN7; X-ray; 2.17 A; A=2-294.
DR PDB; 7NN8; X-ray; 2.27 A; A=2-294.
DR PDB; 7NNB; X-ray; 2.19 A; A=2-294.
DR PDBsum; 2AP9; -.
DR PDBsum; 7NLF; -.
DR PDBsum; 7NLN; -.
DR PDBsum; 7NLO; -.
DR PDBsum; 7NLP; -.
DR PDBsum; 7NLQ; -.
DR PDBsum; 7NLR; -.
DR PDBsum; 7NLS; -.
DR PDBsum; 7NLT; -.
DR PDBsum; 7NLU; -.
DR PDBsum; 7NLW; -.
DR PDBsum; 7NLX; -.
DR PDBsum; 7NLY; -.
DR PDBsum; 7NLZ; -.
DR PDBsum; 7NM0; -.
DR PDBsum; 7NN7; -.
DR PDBsum; 7NN8; -.
DR PDBsum; 7NNB; -.
DR AlphaFoldDB; P9WQ01; -.
DR SMR; P9WQ01; -.
DR STRING; 83332.Rv1654; -.
DR PaxDb; P9WQ01; -.
DR DNASU; 888076; -.
DR GeneID; 888076; -.
DR KEGG; mtu:Rv1654; -.
DR TubercuList; Rv1654; -.
DR eggNOG; COG0548; Bacteria.
DR OMA; EGLYEDW; -.
DR PhylomeDB; P9WQ01; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04250; AAK_NAGK-C; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR HAMAP; MF_00082; ArgB; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR037528; ArgB.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR041727; NAGK-C.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000728; NAGK; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SUPFAM; SSF53633; SSF53633; 1.
DR TIGRFAMs; TIGR00761; argB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Cytoplasm; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..294
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000112637"
FT BINDING 69..70
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 34
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 251
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:7NLY"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:7NLO"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:7NLN"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 207..219
FT /evidence="ECO:0007829|PDB:7NLO"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:7NLO"
FT HELIX 276..282
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:7NLO"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:7NLO"
SQ SEQUENCE 294 AA; 30937 MW; 5EFA44E9E3E8CFC7 CRC64;
MSRIEALPTH IKAQVLAEAL PWLKQLHGKV VVVKYGGNAM TDDTLRRAFA ADMAFLRNCG
IHPVVVHGGG PQITAMLRRL GIEGDFKGGF RVTTPEVLDV ARMVLFGQVG RELVNLINAH
GPYAVGITGE DAQLFTAVRR SVTVDGVATD IGLVGDVDQV NTAAMLDLVA AGRIPVVSTL
APDADGVVHN INADTAAAAV AEALGAEKLL MLTDIDGLYT RWPDRDSLVS EIDTGTLAQL
LPTLESGMVP KVEACLRAVI GGVPSAHIID GRVTHCVLVE LFTDAGTGTK VVRG
