CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006064
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Molybdenum cofactor guanylyltransferase 
Protein Synonyms/Alias
 MoCo guanylyltransferase; GTP:molybdopterin guanylyltransferase; Mo-MPT guanylyltransferase; Molybdopterin guanylyltransferase; Molybdopterin-guanine dinucleotide biosynthesis protein A; Molybdopterin-guanine dinucleotide synthase; MGD synthase; Protein FA 
Gene Name
 mobA 
Gene Synonyms/Alias
 chlB; mob; narB; b3857; JW3829 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
25RRMGGVDKGLLELNGacetylation[1]
175AVDFSDHKDAFVNVNacetylation[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
Functional Description
 Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo- MPT) cofactor (Moco or molybdenum cofactor) to form Mo- molybdopterin guanine dinucleotide (Mo-MGD) cofactor. Is also involved in the biosynthesis of the bis-MGD form of the Moco cofactor (Mo-bisMGD) in which the metal is symmetrically ligated by the dithiolene groups of two MGD molecules. Is necessary and sufficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofactor, which implies formation and efficient insertion of the cofactor into the enzyme without the need of a chaperone. Is specific for GTP since other nucleotides such as ATP and GMP can not be utilized. 
Sequence Annotation
 NP_BIND 12 14 GTP.
 METAL 101 101 Magnesium.
 BINDING 25 25 GTP.
 BINDING 53 53 GTP.
 BINDING 71 71 GTP.
 BINDING 101 101 GTP.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; GTP-binding; Magnesium; Manganese; Metal-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 194 AA 
Protein Sequence
MNLMTTITGV VLAGGKARRM GGVDKGLLEL NGKPLWQHVA DALMTQLSHV VVNANRHQEI 60
YQASGLKVIE DSLADYPGPL AGMLSVMQQE AGEWFLFCPC DTPYIPPDLA ARLNHQRKDA 120
PVVWVHDGER DHPTIALVNR AIEPLLLEYL QAGERRVMVF MRLAGGHAVD FSDHKDAFVN 180
VNTPEELARW QEKR 194 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0070568; F:guanylyltransferase activity; IEA:HAMAP.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. 
Interpro
 IPR025877; MobA-like_NTP_Trfase_dom.
 IPR013482; Molybde_CF_guanTrfase. 
Pfam
 PF12804; NTP_transf_3 
SMART
  
PROSITE
  
PRINTS