ARGC_MYCTU
ID ARGC_MYCTU Reviewed; 352 AA.
AC P9WPZ9; L0T7J2; P63562; P94987;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00150};
DE Short=AGPR {ECO:0000255|HAMAP-Rule:MF_00150};
DE EC=1.2.1.38 {ECO:0000255|HAMAP-Rule:MF_00150};
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150};
DE Short=NAGSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150};
GN Name=argC {ECO:0000255|HAMAP-Rule:MF_00150}; OrderedLocusNames=Rv1652;
GN ORFNames=MTCY06H11.17;
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 AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
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).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC {ECO:0000255|HAMAP-Rule:MF_00150}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate =
CC H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:21588,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00150};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4. {ECO:0000255|HAMAP-
CC Rule:MF_00150}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00150}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00150}.
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DR EMBL; AL123456; CCP44417.1; -; Genomic_DNA.
DR PIR; G70620; G70620.
DR RefSeq; NP_216168.1; NC_000962.3.
DR RefSeq; WP_003898960.1; NZ_NVQJ01000069.1.
DR PDB; 2I3A; X-ray; 2.15 A; A/B/C/D=1-352.
DR PDB; 2I3G; X-ray; 1.85 A; A/B=1-352.
DR PDB; 2NQT; X-ray; 1.58 A; A/B=1-352.
DR PDB; 7NNI; X-ray; 1.54 A; A/B=1-352.
DR PDB; 7NNQ; X-ray; 1.73 A; A/B/C/D=9-352.
DR PDB; 7NNR; X-ray; 1.70 A; A/B=1-352.
DR PDB; 7NOT; X-ray; 2.54 A; A/B/C/D/E/F/G/H=9-352.
DR PDB; 7NPH; X-ray; 2.57 A; A/B/C/D/E/F/G/H=1-352.
DR PDB; 7NPJ; X-ray; 2.81 A; A/B/C/D/E/F/G/H=1-352.
DR PDBsum; 2I3A; -.
DR PDBsum; 2I3G; -.
DR PDBsum; 2NQT; -.
DR PDBsum; 7NNI; -.
DR PDBsum; 7NNQ; -.
DR PDBsum; 7NNR; -.
DR PDBsum; 7NOT; -.
DR PDBsum; 7NPH; -.
DR PDBsum; 7NPJ; -.
DR AlphaFoldDB; P9WPZ9; -.
DR SMR; P9WPZ9; -.
DR STRING; 83332.Rv1652; -.
DR PaxDb; P9WPZ9; -.
DR GeneID; 45425622; -.
DR GeneID; 885278; -.
DR KEGG; mtu:Rv1652; -.
DR TubercuList; Rv1652; -.
DR eggNOG; COG0002; Bacteria.
DR OMA; PHLTPMI; -.
DR PhylomeDB; P9WPZ9; -.
DR BRENDA; 1.2.1.38; 3445.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0070401; F:NADP+ binding; IDA:MTBBASE.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00150; ArgC_type1; 1.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR000706; AGPR_type-1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01850; argC; 1.
DR PROSITE; PS01224; ARGC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..352
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112424"
FT ACT_SITE 158
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:7NNI"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 39..49
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:7NOT"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2I3G"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:7NNI"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:7NNI"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 262..273
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:7NNI"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:7NNI"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:7NNI"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:7NNI"
FT TURN 320..325
FT /evidence="ECO:0007829|PDB:7NNI"
FT HELIX 326..337
FT /evidence="ECO:0007829|PDB:7NNI"
FT TURN 341..344
FT /evidence="ECO:0007829|PDB:7NNI"
SQ SEQUENCE 352 AA; 36304 MW; E7E36B6FC1BAD5CC CRC64;
MQNRQVANAT KVAVAGASGY AGGEILRLLL GHPAYADGRL RIGALTAATS AGSTLGEHHP
HLTPLAHRVV EPTEAAVLGG HDAVFLALPH GHSAVLAQQL SPETLIIDCG ADFRLTDAAV
WERFYGSSHA GSWPYGLPEL PGARDQLRGT RRIAVPGCYP TAALLALFPA LAADLIEPAV
TVVAVSGTSG AGRAATTDLL GAEVIGSARA YNIAGVHRHT PEIAQGLRAV TDRDVSVSFT
PVLIPASRGI LATCTARTRS PLSQLRAAYE KAYHAEPFIY LMPEGQLPRT GAVIGSNAAH
IAVAVDEDAQ TFVAIAAIDN LVKGTAGAAV QSMNLALGWP ETDGLSVVGV AP
