CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005475
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carbamoyl-phosphate synthase pyrimidine-specific large chain 
Protein Synonyms/Alias
 Carbamoyl-phosphate synthetase ammonia chain 
Gene Name
 pyrAB 
Gene Synonyms/Alias
 BSU15520 
Created Date
 July 27, 2013 
Organism
 Bacillus subtilis (strain 168) 
NCBI Taxa ID
 224308 
Lysine Modification
Position
Peptide
Type
References
422ISDELLEKRIKKAGDacetylation[1]
751IDRYLTGKEIEVDAVacetylation[1]
Reference
 [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
 Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG.
 Proteomics. 2013 May;13(10-11):1726-36. [PMID: 23468065
Functional Description
  
Sequence Annotation
 DOMAIN 133 327 ATP-grasp 1.
 DOMAIN 671 861 ATP-grasp 2.
 NP_BIND 159 216 ATP (By similarity).
 NP_BIND 697 754 ATP (By similarity).
 REGION 1 401 Carboxyphosphate synthetic domain.
 REGION 402 546 Oligomerization domain.
 REGION 547 929 Carbamoyl phosphate synthetic domain.
 REGION 930 1071 Allosteric domain.
 METAL 284 284 Magnesium or manganese 1 (By similarity).
 METAL 298 298 Magnesium or manganese 1 (By similarity).
 METAL 298 298 Magnesium or manganese 2 (By similarity).
 METAL 300 300 Magnesium or manganese 2 (By similarity).
 METAL 820 820 Magnesium or manganese 3 (By similarity).
 METAL 832 832 Magnesium or manganese 3 (By similarity).
 METAL 832 832 Magnesium or manganese 4 (By similarity).
 METAL 834 834 Magnesium or manganese 4 (By similarity).  
Keyword
 ATP-binding; Complete proteome; Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1071 AA 
Protein Sequence
MPKRVDINKI LVIGSGPIII GQAAEFDYAG TQACLALKEE GYEVILVNSN PATIMTDTEM 60
ADRVYIEPLT PEFLTRIIRK ERPDAILPTL GGQTGLNLAV ELSERGVLAE CGVEVLGTKL 120
SAIQQAEDRD LFRTLMNELN EPVPESEIIH SLEEAEKFVS QIGFPVIVRP AYTLGGTGGG 180
ICSNETELKE IVENGLKLSP VHQCLLEKSI AGYKEIEYEV MRDSQDHAIV VCNMENIDPV 240
GIHTGDSIVV APSQTLSDRE YQLLRNVSLK LIRALGIEGG CNVQLALDPD SFQYYIIEVN 300
PRVSRSSALA SKATGYPIAK LAAKIAVGLS LDEMMNPVTG KTYAAFEPAL DYVVSKIPRW 360
PFDKFESANR KLGTQMKATG EVMAIGRTLE ESLLKAVRSL EADVYHLELK DAADISDELL 420
EKRIKKAGDE RLFYLAEAYR RGYTVEDLHE FSAIDVFFLH KLFGIVQFEK ELKANAGDTD 480
VLRRAKELGF SDQYISREWK MKESELYSLR KQAGIAPVFK MVDTCAAEFE SETPYFYSTY 540
EEENESVVTD KKSVMVLGSG PIRIGQGVEF DYATVHSVWA IKQAGYEAII VNNNPETVST 600
DFSISDKLYF EPLTIEDVMH IIDLEQPMGV VVQFGGQTAI NLADELSARG VKILGTSLED 660
LDRAEDRDKF EQALGELGVP QPLGKTATSV NQAVSIASDI GYPVLVRPSY VLGGRAMEIV 720
YHEEELLHYM KNAVKINPQH PVLIDRYLTG KEIEVDAVSD GETVVIPGIM EHIERAGVHS 780
GDSIAVYPPQ SLTEDIKKKI EQYTIALAKG LNIVGLLNIQ FVLSQGEVYV LEVNPRSSRT 840
VPFLSKITGI PMANLATKII LGQKLAAFGY TEGLQPEQQG VFVKAPVFSF AKLRRVDITL 900
GPEMKSTGEV MGKDSTLEKA LYKALIASGI QIPNYGSVLL TVADKDKEEG LAIAKRFHAI 960
GYNILATEGT AGYLKEASIP AKVVGKIGQD GPNLLDVIRN GEAQFVINTL TKGKQPARDG 1020
FRIRRESVEN GVACLTSLDT AEAILRVLES MTFRADQMPA VNTNQEAAVT I 1071 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0030145; F:manganese ion binding; IEA:HAMAP.
 GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006526; P:arginine biosynthetic process; IEA:HAMAP. 
Interpro
 IPR011761; ATP-grasp.
 IPR013815; ATP_grasp_subdomain_1.
 IPR013816; ATP_grasp_subdomain_2.
 IPR006275; CarbamoylP_synth_lsu.
 IPR005481; CarbamoylP_synth_lsu_N.
 IPR005480; CarbamoylP_synth_lsu_oligo.
 IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
 IPR005483; CbamoylP_synth_lsu_CPSase_dom.
 IPR011607; MGS-like_dom.
 IPR016185; PreATP-grasp_dom. 
Pfam
 PF00289; CPSase_L_chain
 PF02786; CPSase_L_D2
 PF02787; CPSase_L_D3
 PF02142; MGS 
SMART
 SM01096; CPSase_L_D3
 SM00851; MGS 
PROSITE
 PS50975; ATP_GRASP
 PS00866; CPSASE_1
 PS00867; CPSASE_2 
PRINTS
 PR00098; CPSASE.