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-OCT-2017, entry version 20. 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., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete 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 RT tuberculosis through an interactome, reactome and genome-scale RT 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., RA Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., RA Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., RA Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S., RA Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high RT resolution 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: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) CC + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. CC {ECO:0000255|HAMAP-Rule:MF_00150}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-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_KK339370.1. 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 ProteinModelPortal; P9WPZ9; -. DR SMR; P9WPZ9; -. DR STRING; 83332.Rv1652; -. DR PaxDb; P9WPZ9; -. DR EnsemblBacteria; CCP44417; CCP44417; Rv1652. DR GeneID; 885278; -. DR KEGG; mtu:Rv1652; -. DR TubercuList; Rv1652; -. DR eggNOG; ENOG4105C0N; Bacteria. DR eggNOG; COG0002; LUCA. DR KO; K00145; -. DR OMA; TFVPHLT; -. 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-EC. 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-UniPathway. DR GO; GO:0040007; P:growth; IMP:MTBBASE. 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; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 352 N-acetyl-gamma-glutamyl-phosphate FT reductase. FT /FTId=PRO_0000112424. FT ACT_SITE 158 158 {ECO:0000255|HAMAP-Rule:MF_00150}. FT STRAND 10 15 {ECO:0000244|PDB:2NQT}. FT TURN 16 18 {ECO:0000244|PDB:2NQT}. FT HELIX 20 30 {ECO:0000244|PDB:2NQT}. FT HELIX 33 36 {ECO:0000244|PDB:2NQT}. FT STRAND 39 49 {ECO:0000244|PDB:2NQT}. FT HELIX 55 57 {ECO:0000244|PDB:2NQT}. FT HELIX 63 65 {ECO:0000244|PDB:2NQT}. FT HELIX 75 78 {ECO:0000244|PDB:2NQT}. FT STRAND 82 86 {ECO:0000244|PDB:2NQT}. FT STRAND 90 92 {ECO:0000244|PDB:2I3G}. FT HELIX 94 99 {ECO:0000244|PDB:2NQT}. FT STRAND 104 108 {ECO:0000244|PDB:2NQT}. FT TURN 112 114 {ECO:0000244|PDB:2NQT}. FT HELIX 118 125 {ECO:0000244|PDB:2NQT}. FT HELIX 143 147 {ECO:0000244|PDB:2NQT}. FT STRAND 151 154 {ECO:0000244|PDB:2NQT}. FT HELIX 158 172 {ECO:0000244|PDB:2NQT}. FT STRAND 178 186 {ECO:0000244|PDB:2NQT}. FT HELIX 188 191 {ECO:0000244|PDB:2NQT}. FT HELIX 197 199 {ECO:0000244|PDB:2NQT}. FT HELIX 201 204 {ECO:0000244|PDB:2NQT}. FT TURN 213 216 {ECO:0000244|PDB:2NQT}. FT HELIX 220 228 {ECO:0000244|PDB:2NQT}. FT STRAND 236 243 {ECO:0000244|PDB:2NQT}. FT STRAND 250 257 {ECO:0000244|PDB:2NQT}. FT HELIX 262 273 {ECO:0000244|PDB:2NQT}. FT STRAND 279 281 {ECO:0000244|PDB:2NQT}. FT HELIX 290 292 {ECO:0000244|PDB:2NQT}. FT TURN 293 295 {ECO:0000244|PDB:2NQT}. FT STRAND 299 306 {ECO:0000244|PDB:2NQT}. FT TURN 307 310 {ECO:0000244|PDB:2NQT}. FT STRAND 311 318 {ECO:0000244|PDB:2NQT}. FT TURN 320 325 {ECO:0000244|PDB:2NQT}. FT HELIX 326 337 {ECO:0000244|PDB:2NQT}. FT TURN 341 344 {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 //