ID MOCA_ECOLI Reviewed; 192 AA.
AC Q46810; Q2M9W3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Molybdenum cofactor cytidylyltransferase;
DE Short=MoCo cytidylyltransferase;
DE EC=2.7.7.76;
DE AltName: Full=CTP:molybdopterin cytidylyltransferase;
DE AltName: Full=Mo-MPT cytidylyltransferase;
DE AltName: Full=Molybdopterin cytidylyltransferase;
DE AltName: Full=Molybdopterin-cytosine dinucleotide synthase;
DE Short=MCD synthase;
GN Name=mocA; Synonyms=ygfJ; OrderedLocusNames=b2877, JW2845;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, KINETIC
RP PARAMETERS, GENE NAME, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=19542235; DOI=10.1074/jbc.m109.008565;
RA Neumann M., Mittelstadt G., Seduk F., Iobbi-Nivol C., Leimkuhler S.;
RT "MocA is a specific cytidylyltransferase involved in molybdopterin cytosine
RT dinucleotide biosynthesis in Escherichia coli.";
RL J. Biol. Chem. 284:21891-21898(2009).
RN [4]
RP DOMAIN, INTERACTION WITH PAOD, AND MUTAGENESIS OF 9-THR--ALA-11 AND
RP 79-LEU--SER-82.
RX PubMed=21081498; DOI=10.1074/jbc.m110.155671;
RA Neumann M., Seduk F., Iobbi-Nivol C., Leimkuhler S.;
RT "Molybdopterin dinucleotide biosynthesis in Escherichia coli:
RT identification of amino acid residues of molybdopterin dinucleotide
RT transferases that determine specificity for binding of guanine or cytosine
RT nucleotides.";
RL J. Biol. Chem. 286:1400-1408(2011).
CC -!- FUNCTION: Transfers a CMP moiety from CTP to Mo-molybdopterin (Mo-MPT)
CC cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin
CC cytosine dinucleotide (Mo-MCD) cofactor. Is specific for CTP; other
CC nucleotides such as ATP and GTP cannot be utilized. Is also able to
CC convert MPT to MCD in the absence of molybdate, however, with only one
CC catalytic turnover. {ECO:0000269|PubMed:19542235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin
CC cytosine dinucleotide; Xref=Rhea:RHEA:31335, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:71302,
CC ChEBI:CHEBI:71308; EC=2.7.7.76;
CC Evidence={ECO:0000269|PubMed:19542235};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19542235};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19542235};
CC Note=Mg(2+) is essential for activity. However, Mn(2+) is able to
CC functionally replace Mg(2+) with a 50% reduced efficiency, whereas no
CC MCD is produced with other divalent cations like Co(2+) or Ni(2+).
CC {ECO:0000269|PubMed:19542235};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 uM for CTP {ECO:0000269|PubMed:19542235};
CC -!- SUBUNIT: Monomer. Interacts with the Moco-binding chaperone PaoD.
CC {ECO:0000269|PubMed:19542235, ECO:0000269|PubMed:21081498}.
CC -!- DOMAIN: The N-terminal domain determines nucleotide recognition and
CC specific binding, while the C-terminal domain determines the specific
CC binding to the target protein. When the N-terminal domain of MobA is
CC fused to the C-terminal domain of MocA, comparable kinetic constants as
CC wild-type MobA are obtained with GTP, and the activity with CTP is
CC completely lost. Consistent results are obtained when the N-terminal
CC domain of MocA is fused to the C-terminal domain of MobA: the kinetic
CC constants with CTP are comparable with the ones found for wild-type
CC MocA, although no activity with GTP is detected.
CC {ECO:0000269|PubMed:21081498}.
CC -!- DISRUPTION PHENOTYPE: A disruption in the mocA gene impairs MCD
CC biosynthesis in E.coli, resulting in an inactive PaoABC aldehyde
CC oxidoreductase devoid of MCD cofactor. {ECO:0000269|PubMed:19542235}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U28375; AAA83058.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75915.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76943.1; -; Genomic_DNA.
DR PIR; E65071; E65071.
DR RefSeq; NP_417353.1; NC_000913.3.
DR RefSeq; WP_001272828.1; NZ_LN832404.1.
DR AlphaFoldDB; Q46810; -.
DR SMR; Q46810; -.
DR BioGRID; 4259705; 103.
DR IntAct; Q46810; 2.
DR STRING; 511145.b2877; -.
DR PaxDb; 511145-b2877; -.
DR EnsemblBacteria; AAC75915; AAC75915; b2877.
DR GeneID; 947356; -.
DR KEGG; ecj:JW2845; -.
DR KEGG; eco:b2877; -.
DR PATRIC; fig|1411691.4.peg.3857; -.
DR EchoBASE; EB2872; -.
DR eggNOG; COG2068; Bacteria.
DR HOGENOM; CLU_061980_1_2_6; -.
DR InParanoid; Q46810; -.
DR OMA; KHPPLID; -.
DR OrthoDB; 5298023at2; -.
DR PhylomeDB; Q46810; -.
DR BioCyc; EcoCyc:G7496-MONOMER; -.
DR BioCyc; MetaCyc:G7496-MONOMER; -.
DR SABIO-RK; Q46810; -.
DR PRO; PR:Q46810; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0061602; F:molybdenum cofactor cytidylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:1902760; P:Mo(VI)-molybdopterin cytosine dinucleotide biosynthetic process; IDA:EcoCyc.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IMP:EcoCyc.
DR CDD; cd04182; GT_2_like_f; 1.
DR InterPro; IPR017696; Mo_hydrolase_YgfJ.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR03310; matur_MocA_YgfJ; 1.
DR PANTHER; PTHR43777; MOLYBDENUM COFACTOR CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR43777:SF1; MOLYBDENUM COFACTOR CYTIDYLYLTRANSFERASE; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 1: Evidence at protein level;
KW Magnesium; Manganese; Metal-binding; Molybdenum cofactor biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..192
FT /note="Molybdenum cofactor cytidylyltransferase"
FT /id="PRO_0000169355"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 9..11
FT /note="TAA->LAG: 12-fold decrease in affinity for CTP and
FT 3-fold decrease in catalytic activity. Displays a 3-fold
FT decrease in activity with CTP and gains a low activity with
FT GTP as substrate; when associated with 79-P--G-82."
FT /evidence="ECO:0000269|PubMed:21081498"
FT MUTAGEN 79..82
FT /note="LLTS->PLAG: 15-fold decrease in affinity for CTP and
FT 1.5-fold decrease in catalytic activity. Displays a 3-fold
FT decrease in activity with CTP and gains a low activity with
FT GTP as substrate; when associated with 9-L--G-11."
FT /evidence="ECO:0000269|PubMed:21081498"
SQ SEQUENCE 192 AA; 21514 MW; 5F8E4CDE6133ECD6 CRC64;
MSAIDCIITA AGLSSRMGQW KMMLPWEQGT ILDTSIKNAL QFCSRIILVT GYRGNELHER
YANQSNITII HNPDYAQGLL TSVKAAVPAV QTEHCFLTHG DMPTLTIDIF RKIWSLRNDG
AILPLHNGIP GHPILVSKPC LMQAIQRPNV TNMRQALLMG DHYSVEIENA EIILDIDTPD
DFITAKERYT EI
//
