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 07-OCT-2020, entry version 31. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDBsum; 2I3A; -. DR PDBsum; 2I3G; -. DR PDBsum; 2NQT; -. DR SMR; P9WPZ9; -. DR STRING; 83332.Rv1652; -. DR PaxDb; P9WPZ9; -. DR EnsemblBacteria; CCP44417; CCP44417; Rv1652. DR GeneID; 23492182; -. DR GeneID; 885278; -. DR KEGG; mtu:Rv1652; -. DR KEGG; mtv:RVBD_1652; -. DR TubercuList; Rv1652; -. DR eggNOG; COG0002; Bacteria. DR KO; K00145; -. DR OMA; PHLTPMI; -. DR PhylomeDB; P9WPZ9; -. 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:0000244|PDB:2NQT" FT TURN 16..18 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 20..30 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 33..36 FT /evidence="ECO:0000244|PDB:2NQT" FT STRAND 39..49 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 55..57 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 63..65 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 75..78 FT /evidence="ECO:0000244|PDB:2NQT" FT STRAND 82..86 FT /evidence="ECO:0000244|PDB:2NQT" FT STRAND 90..92 FT /evidence="ECO:0000244|PDB:2I3G" FT HELIX 94..99 FT /evidence="ECO:0000244|PDB:2NQT" FT STRAND 104..108 FT /evidence="ECO:0000244|PDB:2NQT" FT TURN 112..114 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 118..125 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 143..147 FT /evidence="ECO:0000244|PDB:2NQT" FT STRAND 151..154 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 158..172 FT /evidence="ECO:0000244|PDB:2NQT" FT STRAND 178..186 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 188..191 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 197..199 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 201..204 FT /evidence="ECO:0000244|PDB:2NQT" FT TURN 213..216 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 220..228 FT /evidence="ECO:0000244|PDB:2NQT" FT STRAND 236..243 FT /evidence="ECO:0000244|PDB:2NQT" FT STRAND 250..257 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 262..273 FT /evidence="ECO:0000244|PDB:2NQT" FT STRAND 279..281 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 290..292 FT /evidence="ECO:0000244|PDB:2NQT" FT TURN 293..295 FT /evidence="ECO:0000244|PDB:2NQT" FT STRAND 299..306 FT /evidence="ECO:0000244|PDB:2NQT" FT TURN 307..310 FT /evidence="ECO:0000244|PDB:2NQT" FT STRAND 311..318 FT /evidence="ECO:0000244|PDB:2NQT" FT TURN 320..325 FT /evidence="ECO:0000244|PDB:2NQT" FT HELIX 326..337 FT /evidence="ECO:0000244|PDB:2NQT" FT TURN 341..344 FT /evidence="ECO:0000244|PDB:2NQT" 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 //