CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001857
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carbamoyl-phosphate synthase large chain 
Protein Synonyms/Alias
 Carbamoyl-phosphate synthetase ammonia chain 
Gene Name
 carB 
Gene Synonyms/Alias
 pyrA; b0033; JW0031 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
202GLDLSPTKELLIDESacetylation[1]
291VQFAVNPKNGRLIVIacetylation[1]
366IPRFNFEKFAGANDRacetylation[1]
412GATGFDPKVSLDDPEacetylation[1]
423DDPEALTKIRRELKDacetylation[1]
429TKIRRELKDAGADRIacetylation[1]
475ELVRLEEKVAEVGITacetylation[1]
504FADARLAKLAGVREAacetylation[1]
527YDLHPVYKRVDTCAAacetylation[1]
636IVRIEKPKGVIVQYGacetylation[1]
649YGGQTPLKLARALEAacetylation[1]
704AIEMAVEKAKEIGYPacetylation[1]
706EMAVEKAKEIGYPLVacetylation[1]
815VMRQQVQKLAFELQVacetylation[1]
881LAEQGVTKEVIPPYYacetylation[1]
891IPPYYSVKEVVLPFNacetylation[1]
899EVVLPFNKFPGVDPLacetylation[1]
963RVVDLAAKLLKQGFEacetylation[1, 2]
966DLAAKLLKQGFELDAacetylation[1]
993INPRLVNKVHEGRPHacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508] 
Functional Description
  
Sequence Annotation
 DOMAIN 133 328 ATP-grasp 1.
 DOMAIN 679 870 ATP-grasp 2.
 NP_BIND 159 216 ATP (By similarity).
 NP_BIND 705 762 ATP (By similarity).
 REGION 2 403 Carboxyphosphate synthetic domain.
 REGION 404 553 Oligomerization domain.
 REGION 554 936 Carbamoyl phosphate synthetic domain.
 REGION 937 1073 Allosteric domain.
 METAL 285 285 Manganese 1.
 METAL 299 299 Manganese 1.
 METAL 299 299 Manganese 2.
 METAL 301 301 Manganese 2.
 METAL 829 829 Manganese 3.
 METAL 841 841 Manganese 3.
 METAL 841 841 Manganese 4 (By similarity).
 METAL 843 843 Manganese 4 (By similarity).  
Keyword
 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Manganese; Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1073 AA 
Protein Sequence
MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM 60
ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLEE FGVTMIGATA 120
DAIDKAEDRR RFDVAMKKIG LETARSGIAH TMEEALAVAA DVGFPCIIRP SFTMGGSGGG 180
IAYNREEFEE ICARGLDLSP TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM 240
GIHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM 300
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP SIDYVVTKIP 360
RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR GLEVGATGFD PKVSLDDPEA 420
LTKIRRELKD AGADRIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEKVAEVG 480
ITGLNADFLR QLKRKGFADA RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT 540
AYMYSTYEEE CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN 600
CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL ARALEAAGVP 660
VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTAIEM AVEKAKEIGY PLVVRPSYVL 720
GGRAMEIVYD EADLRRYFQT AVSVSNDAPV LLDHFLDDAV EVDVDAICDG EMVLIGGIME 780
HIEQAGVHSG DSACSLPAYT LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI 840
EVNPRAARTV PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF 900
PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR EGDKERVVDL 960
AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIINTTSGR 1020
RAIEDSRVIR RSALQYKVHY DTTLNGGFAT AMALNADATE KVISVQEMHA QIK 1073 
Gene Ontology
 GO:0005951; C:carbamoyl-phosphate synthase complex; IDA:EcoCyc.
 GO:0016597; F:amino acid binding; IDA:EcoliWiki.
 GO:0005524; F:ATP binding; IDA:EcoCyc.
 GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IDA:EcoliWiki.
 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:0046872; F:metal ion binding; IDA:EcoliWiki.
 GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
 GO:0008652; P:cellular amino acid biosynthetic process; IMP:EcoliWiki.
 GO:0019856; P:pyrimidine nucleobase biosynthetic process; IMP:EcoliWiki. 
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.