※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carbamoyl-phosphate synthase large chain
Protein Synonyms/Alias
 
Gene Name
 carB
Gene Synonyms/Alias
 Z0038, ECs0036
Created Date
 3-June-2014
Organism
 Escherichia coli O157:H7
NCBI Taxa ID
 83334
Phosphorylation
Position
Peptide
Code
Type
References
330 AAKLAVGYTLDELMN Y HTP [1]
Reference
 [1]The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence.
 Hansen AM,Chaerkady R,Sharma J,Díaz-Mejía JJ,Tyagi N,Renuse S,Jacob HK,Pinto SM,Sahasrabuddhe NA,Kim MS,Delanghe B,Srinivasan N,Emili A,Kaper JB,Pandey A
 PLoS Pathog. 2013;9(6):e1003403. [PMID:23785281]
Functional Description From UniProt
 
Sequence Annotation From UniProt
 
Key Word From UniProt
 Amino-acidbiosynthesis; Argininebiosynthesis; ATP-binding; Completeproteome; Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; Pyrimidinebiosynthesis; Repeat
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 AGAERIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEKVAEVG 480
 ITGLNAEFLR QLKRKGFADA RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT 540
 AYMYSTYEEE CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN 600
 CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL ARALEAAGVP 660
 VIGTSPDAID RAEDRERFQH AVDRLKLKQP 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
  GO:0005524   F:ATP binding IEA:UniProtKB-HAMAP
  GO:0004088   F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity IEA:UniProtKB-HAMAP
  GO:0000287   F:magnesium ion binding IEA:UniProtKB-HAMAP
  GO:0030145   F:manganese ion binding IEA:UniProtKB-HAMAP
  GO:0044205   P:'de novo' UMP biosynthetic process IEA:UniProtKB-UniPathway
  GO:0006526   P:arginine biosynthetic process IEA:UniProtKB-HAMAP
  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.
  PF00289   CPSase_L_chain.
  PF02786   CPSase_L_D2.
  PF02787   CPSase_L_D3.
  PF02142   MGS.
  SM01096   CPSase_L_D3.
  SM00851   MGS.
  PS50975   ATP_GRASP.
  PS00866   CPSASE_1.
  PS00867   CPSASE_2.
  PR00098   CPSASE.