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Molybdenum cofactor guanylyltransferase (MoCo guanylyltransferase) (EC 2.7.7.77) (GTP:molybdopterin guanylyltransferase) (Mo-MPT guanylyltransferase) (Molybdopterin guanylyltransferase) (Molybdopterin-guanine dinucleotide biosynthesis protein A) (Molybdopterin-guanine dinucleotide synthase) (MGD synthase) (Protein FA)

 MOBA_ECOLI              Reviewed;         194 AA.
P32173; Q2M8F5; Q9LBV0;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
05-JUL-2017, entry version 143.
RecName: Full=Molybdenum cofactor guanylyltransferase;
Short=MoCo guanylyltransferase;
EC=2.7.7.77;
AltName: Full=GTP:molybdopterin guanylyltransferase;
AltName: Full=Mo-MPT guanylyltransferase;
AltName: Full=Molybdopterin guanylyltransferase;
AltName: Full=Molybdopterin-guanine dinucleotide biosynthesis protein A;
AltName: Full=Molybdopterin-guanine dinucleotide synthase;
Short=MGD synthase;
AltName: Full=Protein FA;
Name=mobA; Synonyms=chlB, mob, narB; OrderedLocusNames=b3857, JW3829;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=8346018; DOI=10.1093/nar/21.15.3391;
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
"Analysis of the Escherichia coli genome. III. DNA sequence of the
region from 87.2 to 89.2 minutes.";
Nucleic Acids Res. 21:3391-3398(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=K12;
PubMed=7551035; DOI=10.1099/13500872-141-7-1663;
Iobbi-Nivol C., Palmer T., Whitty P.W., McNairn E., Boxer D.H.;
"The mob locus of Escherichia coli K12 required for molybdenum
cofactor biosynthesis is expressed at very low levels.";
Microbiology 141:1663-1671(1995).
[5]
PROTEIN SEQUENCE OF 1-5, FUNCTION IN MGD BIOSYNTHESIS, AND SUBUNIT.
PubMed=8020507; DOI=10.1111/j.1432-1033.1994.tb18913.x;
Palmer T., Vasishta A., Whitty P.W., Boxer D.H.;
"Isolation of protein FA, a product of the mob locus required for
molybdenum cofactor biosynthesis in Escherichia coli.";
Eur. J. Biochem. 222:687-692(1994).
[6]
FUNCTION IN MGD BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
STRAIN=RK4353;
PubMed=1648082;
Johnson J.L., Indermaur L.W., Rajagopalan K.V.;
"Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of
the chlB gene product for the formation of molybdopterin guanine
dinucleotide.";
J. Biol. Chem. 266:12140-12145(1991).
[7]
FUNCTION IN BIS(MGD) AND MGD BIOSYNTHESIS, CATALYTIC ACTIVITY,
SUBSTRATE SPECIFICITY, AND COFACTOR.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=10978348; DOI=10.1074/jbc.M007407200;
Temple C.A., Rajagopalan K.V.;
"Mechanism of assembly of the bis(molybdopterin guanine
dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl
sulfoxide reductase.";
J. Biol. Chem. 275:40202-40210(2000).
[8]
INTERACTION WITH MOEA AND MOBB.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=12372836; DOI=10.1074/jbc.M205806200;
Magalon A., Frixon C., Pommier J., Giordano G., Blasco F.;
"In vivo interactions between gene products involved in the final
stages of molybdenum cofactor biosynthesis in Escherichia coli.";
J. Biol. Chem. 277:48199-48204(2002).
[9]
FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, DOMAIN, AND
MUTAGENESIS OF 12-LEU--GLY-14 AND 79-PRO--GLY-82.
PubMed=21081498; DOI=10.1074/jbc.M110.155671;
Neumann M., Seduk F., Iobbi-Nivol C., Leimkuhler S.;
"Molybdopterin dinucleotide biosynthesis in Escherichia coli:
identification of amino acid residues of molybdopterin dinucleotide
transferases that determine specificity for binding of guanine or
cytosine nucleotides.";
J. Biol. Chem. 286:1400-1408(2011).
[10]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX
WITH MN-GTP, COFACTOR, AND SUBUNIT.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=10978347; DOI=10.1074/jbc.M007406200;
Lake M.W., Temple C.A., Rajagopalan K.V., Schindelin H.;
"The crystal structure of the Escherichia coli MobA protein provides
insight into molybdopterin guanine dinucleotide biosynthesis.";
J. Biol. Chem. 275:40211-40217(2000).
[11]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
STRAIN=K12;
PubMed=11080634; DOI=10.1016/S0969-2126(00)00518-9;
Stevenson C.E., Sargent F., Buchanan G., Palmer T., Lawson D.M.;
"Crystal structure of the molybdenum cofactor biosynthesis protein
MobA from Escherichia coli at near-atomic resolution.";
Structure 8:1115-1125(2000).
[12]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF MUTANTS ALA-19; LEU-22;
ASN-101; ASP-180 AND ASP-182, AND MUTAGENESIS OF GLY-15; ARG-19;
GLY-22; LYS-25; GLY-78; GLY-82; ASP-101; ARG-156; ASN-180 AND ASN-182.
STRAIN=K12;
PubMed=12719427; DOI=10.1074/jbc.M302639200;
Guse A., Stevenson C.E., Kuper J., Buchanan G., Schwarz G.,
Giordano G., Magalon A., Mendel R.R., Lawson D.M., Palmer T.;
"Biochemical and structural analysis of the molybdenum cofactor
biosynthesis protein MobA.";
J. Biol. Chem. 278:25302-25307(2003).
-!- FUNCTION: 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 cannot be utilized.
{ECO:0000269|PubMed:10978348, ECO:0000269|PubMed:1648082,
ECO:0000269|PubMed:21081498, ECO:0000269|PubMed:8020507}.
-!- CATALYTIC ACTIVITY: GTP + molybdenum cofactor = diphosphate +
guanylyl molybdenum cofactor. {ECO:0000269|PubMed:10978348,
ECO:0000269|PubMed:21081498}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10978347,
ECO:0000269|PubMed:10978348};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:10978347,
ECO:0000269|PubMed:10978348};
Note=Both divalent cations appear to be equally efficient in an
vitro reconstitution assay. {ECO:0000269|PubMed:10978347,
ECO:0000269|PubMed:10978348};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.5 uM for GTP {ECO:0000269|PubMed:21081498};
-!- SUBUNIT: Monomer. An equilibrium exists between a monomeric and
oligomeric form of the enzyme, which could be an octamer; whether
this oligomeric arrangement is of functional relevance is unclear.
Interacts with MoeA and MobB in vivo.
{ECO:0000269|PubMed:10978347, ECO:0000269|PubMed:12372836,
ECO:0000269|PubMed:8020507}.
-!- INTERACTION:
P12281:moeA; NbExp=3; IntAct=EBI-1133881, EBI-554393;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- INDUCTION: Is expressed at very low levels under both aerobic and
anaerobic growth conditions. {ECO:0000269|PubMed:7551035}.
-!- DOMAIN: The N-terminal domain determines nucleotide recognition
and specific binding, while the C-terminal domain determines the
specific binding to the target protein. When the N-terminal domain
of MobA is fused to the C-terminal domain of MocA, comparable
kinetic constants as wild-type MobA are obtained with GTP, and the
activity with CTP is completely lost. Consistent results are
obtained when the N-terminal domain of MocA is fused to the C-
terminal domain of MobA: the kinetic constants with CTP are
comparable with the ones found for wild-type MocA, although no
activity with GTP is detected. {ECO:0000269|PubMed:21081498}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene are chlorate-
resistant, fail to synthesize MGD and accumulate elevated
quantities of MPT. {ECO:0000269|PubMed:1648082}.
-!- SIMILARITY: Belongs to the MobA family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L19201; AAB02992.1; -; Genomic_DNA.
EMBL; U00096; AAC76855.1; -; Genomic_DNA.
EMBL; AP009048; BAE77451.1; -; Genomic_DNA.
PIR; S40803; S40803.
RefSeq; NP_418294.1; NC_000913.3.
RefSeq; WP_001052181.1; NZ_LN832404.1.
PDB; 1E5K; X-ray; 1.35 A; A=1-194.
PDB; 1FR9; X-ray; 1.65 A; A=1-194.
PDB; 1FRW; X-ray; 1.75 A; A=1-194.
PDB; 1H4C; X-ray; 1.65 A; A=1-194.
PDB; 1H4D; X-ray; 1.74 A; A=1-194.
PDB; 1H4E; X-ray; 1.65 A; A=1-194.
PDB; 1HJJ; X-ray; 1.65 A; A=1-194.
PDB; 1HJL; X-ray; 2.00 A; A=1-194.
PDBsum; 1E5K; -.
PDBsum; 1FR9; -.
PDBsum; 1FRW; -.
PDBsum; 1H4C; -.
PDBsum; 1H4D; -.
PDBsum; 1H4E; -.
PDBsum; 1HJJ; -.
PDBsum; 1HJL; -.
ProteinModelPortal; P32173; -.
SMR; P32173; -.
DIP; DIP-10233N; -.
IntAct; P32173; 10.
MINT; MINT-1232345; -.
STRING; 316385.ECDH10B_4046; -.
DrugBank; DB04272; Citric Acid.
DrugBank; DB04137; Guanosine-5'-Triphosphate.
PaxDb; P32173; -.
PRIDE; P32173; -.
EnsemblBacteria; AAC76855; AAC76855; b3857.
EnsemblBacteria; BAE77451; BAE77451; BAE77451.
GeneID; 948349; -.
KEGG; ecj:JW3829; -.
KEGG; eco:b3857; -.
PATRIC; fig|1411691.4.peg.2858; -.
EchoBASE; EB1776; -.
EcoGene; EG11829; mobA.
eggNOG; ENOG4105C6R; Bacteria.
eggNOG; COG0746; LUCA.
HOGENOM; HOG000280423; -.
InParanoid; P32173; -.
KO; K03752; -.
PhylomeDB; P32173; -.
BioCyc; EcoCyc:EG11829-MONOMER; -.
BioCyc; MetaCyc:EG11829-MONOMER; -.
BRENDA; 2.7.7.77; 2026.
EvolutionaryTrace; P32173; -.
PRO; PR:P32173; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
GO; GO:0061603; F:molybdenum cofactor guanylyltransferase activity; IDA:EcoCyc.
GO; GO:1902758; P:bis(molybdopterin guanine dinucleotide)molybdenum biosynthetic process; IMP:EcoCyc.
CDD; cd02503; MobA; 1.
Gene3D; 3.90.550.10; -; 1.
HAMAP; MF_00316; MobA; 1.
InterPro; IPR025877; MobA-like_NTP_Trfase.
InterPro; IPR013482; Molybde_CF_guanTrfase.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
PANTHER; PTHR19136:SF85; PTHR19136:SF85; 1.
Pfam; PF12804; NTP_transf_3; 1.
SUPFAM; SSF53448; SSF53448; 1.
TIGRFAMs; TIGR02665; molyb_mobA; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
GTP-binding; Magnesium; Manganese; Metal-binding;
Molybdenum cofactor biosynthesis; Nucleotide-binding;
Reference proteome; Transferase.
CHAIN 1 194 Molybdenum cofactor guanylyltransferase.
/FTId=PRO_0000134887.
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.
MUTAGEN 12 14 LAG->TAA: 7.5-fold decrease in affinity
for GTP and nearly no effect on catalytic
activity. Displays a 3-fold decrease in
activity with GTP and gains a low
activity with CTP as substrate; when
associated with 79-LLTS-82.
{ECO:0000269|PubMed:21081498}.
MUTAGEN 15 15 G->L: Complete loss of catalytic
activity. Still capable of binding MPT
and MGD and interacting with both MoeA
and MobB. {ECO:0000269|PubMed:12719427}.
MUTAGEN 19 19 R->A: Slight reduction in catalytic
activity. {ECO:0000269|PubMed:12719427}.
MUTAGEN 22 22 G->L: Nearly no effect on catalytic
activity. {ECO:0000269|PubMed:12719427}.
MUTAGEN 25 25 K->A: Marked reduction in catalytic
activity. Still capable of interacting
with both MoeA and MobB.
{ECO:0000269|PubMed:12719427}.
MUTAGEN 78 78 G->L: Nearly no effect on catalytic
activity. {ECO:0000269|PubMed:12719427}.
MUTAGEN 79 82 PLAG->LLTS: 11-fold decrease in affinity
for GTP and nearly no effect on catalytic
activity. Displays a 3-fold decrease in
activity with GTP and gains a low
activity with CTP as substrate; when
associated with 12-TAA-14.
{ECO:0000269|PubMed:21081498}.
MUTAGEN 82 82 G->L: Slight reduction in catalytic
activity. {ECO:0000269|PubMed:12719427}.
MUTAGEN 101 101 D->A: Complete loss of catalytic
activity. {ECO:0000269|PubMed:12719427}.
MUTAGEN 101 101 D->N: Marked reduction in catalytic
activity. Still capable of interacting
with both MoeA and MobB.
{ECO:0000269|PubMed:12719427}.
MUTAGEN 156 156 R->A: Nearly no effect on catalytic
activity. {ECO:0000269|PubMed:12719427}.
MUTAGEN 180 180 N->D: Nearly no effect on catalytic
activity. {ECO:0000269|PubMed:12719427}.
MUTAGEN 182 182 N->D: Nearly no effect on catalytic
activity. {ECO:0000269|PubMed:12719427}.
HELIX 3 5 {ECO:0000244|PDB:1FR9}.
STRAND 6 12 {ECO:0000244|PDB:1E5K}.
STRAND 18 20 {ECO:0000244|PDB:1E5K}.
HELIX 25 27 {ECO:0000244|PDB:1E5K}.
STRAND 28 30 {ECO:0000244|PDB:1E5K}.
HELIX 35 46 {ECO:0000244|PDB:1E5K}.
STRAND 50 53 {ECO:0000244|PDB:1E5K}.
STRAND 55 57 {ECO:0000244|PDB:1E5K}.
HELIX 58 62 {ECO:0000244|PDB:1E5K}.
STRAND 67 69 {ECO:0000244|PDB:1FR9}.
HELIX 79 89 {ECO:0000244|PDB:1E5K}.
STRAND 92 99 {ECO:0000244|PDB:1E5K}.
HELIX 109 115 {ECO:0000244|PDB:1E5K}.
TURN 116 119 {ECO:0000244|PDB:1FR9}.
STRAND 121 126 {ECO:0000244|PDB:1E5K}.
STRAND 131 139 {ECO:0000244|PDB:1E5K}.
HELIX 142 151 {ECO:0000244|PDB:1E5K}.
HELIX 157 163 {ECO:0000244|PDB:1E5K}.
STRAND 167 170 {ECO:0000244|PDB:1E5K}.
TURN 175 178 {ECO:0000244|PDB:1E5K}.
HELIX 184 188 {ECO:0000244|PDB:1E5K}.
SEQUENCE 194 AA; 21643 MW; B79B32DD7348DD48 CRC64;
MNLMTTITGV VLAGGKARRM GGVDKGLLEL NGKPLWQHVA DALMTQLSHV VVNANRHQEI
YQASGLKVIE DSLADYPGPL AGMLSVMQQE AGEWFLFCPC DTPYIPPDLA ARLNHQRKDA
PVVWVHDGER DHPTIALVNR AIEPLLLEYL QAGERRVMVF MRLAGGHAVD FSDHKDAFVN
VNTPEELARW QEKR


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