MOAC_ECOLI
ID MOAC_ECOLI Reviewed; 161 AA.
AC P0A738; P30747; P77530;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01224, ECO:0000305};
DE EC=4.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01224, ECO:0000269|PubMed:25941396};
DE AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000255|HAMAP-Rule:MF_01224};
GN Name=moaC; Synonyms=chlA3; OrderedLocusNames=b0783, JW0766;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8361352; DOI=10.1111/j.1365-2958.1993.tb01652.x;
RA Rivers S.L., McNairn E., Blasco F., Giordano G., Boxer D.H.;
RT "Molecular genetic analysis of the moa operon of Escherichia coli K-12
RT required for molybdenum cofactor biosynthesis.";
RL Mol. Microbiol. 8:1071-1081(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10903949; DOI=10.1016/s0969-2126(00)00157-x;
RA Wuebbens M.M., Liu M.T.W., Rajagopalan K.V., Schindelin H.;
RT "Insights into molybdenum cofactor deficiency provided by the crystal
RT structure of the molybdenum cofactor biosynthesis protein MoaC.";
RL Structure 8:709-718(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 3-161 IN COMPLEX WITH
RP (8S)-3',8-CYCLO-7,8-DIHYDROGUANOSINE 5'-TRIPHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF ASP-17; LYS-21; ARG-26; LYS-51; HIS-77; GLU-112;
RP GLU-114; ASP-128; LYS-131 AND LYS-147, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP REACTION MECHANISM.
RX PubMed=25941396; DOI=10.1073/pnas.1500697112;
RA Hover B.M., Tonthat N.K., Schumacher M.A., Yokoyama K.;
RT "Mechanism of pyranopterin ring formation in molybdenum cofactor
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:6347-6352(2015).
CC -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC (cPMP). {ECO:0000255|HAMAP-Rule:MF_01224, ECO:0000269|PubMed:25941396}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic
CC pyranopterin phosphate + diphosphate; Xref=Rhea:RHEA:49580,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59648, ChEBI:CHEBI:131766;
CC EC=4.6.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01224,
CC ECO:0000269|PubMed:25941396};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.21 uM for (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate
CC {ECO:0000269|PubMed:25941396};
CC Note=kcat is 0.56 min(-1). {ECO:0000269|PubMed:25941396};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01224}.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_01224, ECO:0000269|PubMed:25941396}.
CC -!- INTERACTION:
CC P0A738; P0A7L0: rplA; NbExp=2; IntAct=EBI-554314, EBI-543771;
CC -!- INDUCTION: By anaerobiosis, repressed by the molybdenum cofactor.
CC -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000255|HAMAP-
CC Rule:MF_01224}.
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DR EMBL; X70420; CAA49863.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73870.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35441.1; -; Genomic_DNA.
DR PIR; G64814; G64814.
DR RefSeq; NP_415304.1; NC_000913.3.
DR RefSeq; WP_000080885.1; NZ_STEB01000028.1.
DR PDB; 1EKR; X-ray; 2.00 A; A=1-161.
DR PDB; 1EKS; X-ray; 2.50 A; A=1-161.
DR PDB; 4PYA; X-ray; 1.79 A; A=3-161.
DR PDB; 4PYD; X-ray; 3.19 A; A/B/C/D/E/F=1-161.
DR PDBsum; 1EKR; -.
DR PDBsum; 1EKS; -.
DR PDBsum; 4PYA; -.
DR PDBsum; 4PYD; -.
DR AlphaFoldDB; P0A738; -.
DR SMR; P0A738; -.
DR BioGRID; 4262176; 46.
DR DIP; DIP-10230N; -.
DR IntAct; P0A738; 20.
DR STRING; 511145.b0783; -.
DR jPOST; P0A738; -.
DR PaxDb; P0A738; -.
DR PRIDE; P0A738; -.
DR EnsemblBacteria; AAC73870; AAC73870; b0783.
DR EnsemblBacteria; BAA35441; BAA35441; BAA35441.
DR GeneID; 67413822; -.
DR GeneID; 945397; -.
DR KEGG; ecj:JW0766; -.
DR KEGG; eco:b0783; -.
DR PATRIC; fig|1411691.4.peg.1495; -.
DR EchoBASE; EB1617; -.
DR eggNOG; COG0315; Bacteria.
DR HOGENOM; CLU_074693_1_1_6; -.
DR InParanoid; P0A738; -.
DR OMA; IWDMVKS; -.
DR PhylomeDB; P0A738; -.
DR BioCyc; EcoCyc:EG11666-MON; -.
DR BioCyc; MetaCyc:EG11666-MON; -.
DR BRENDA; 4.6.1.17; 2026.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; P0A738; -.
DR PRO; PR:P0A738; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IMP:EcoCyc.
DR CDD; cd01420; MoaC_PE; 1.
DR Gene3D; 3.30.70.640; -; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR023045; Mo_CF_biosynth-C.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR Pfam; PF01967; MoaC; 1.
DR SUPFAM; SSF55040; SSF55040; 1.
DR TIGRFAMs; TIGR00581; moaC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase;
KW Molybdenum cofactor biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8361352"
FT CHAIN 2..161
FT /note="Cyclic pyranopterin monophosphate synthase"
FT /id="PRO_0000097798"
FT ACT_SITE 128
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 75..77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224,
FT ECO:0000269|PubMed:25941396"
FT BINDING 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224,
FT ECO:0000269|PubMed:25941396"
FT MUTAGEN 17
FT /note="D->A: Loss of activity by 70%."
FT /evidence="ECO:0000269|PubMed:25941396"
FT MUTAGEN 21
FT /note="K->A: Loss of activity by 85%."
FT /evidence="ECO:0000269|PubMed:25941396"
FT MUTAGEN 26
FT /note="R->A: Loss of activity by 80%."
FT /evidence="ECO:0000269|PubMed:25941396"
FT MUTAGEN 51
FT /note="K->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:25941396"
FT MUTAGEN 52
FT /note="G->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:10903949"
FT MUTAGEN 67
FT /note="K->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:10903949"
FT MUTAGEN 76
FT /note="C->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:10903949"
FT MUTAGEN 77
FT /note="H->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:25941396"
FT MUTAGEN 112
FT /note="E->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:25941396"
FT MUTAGEN 114
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25941396"
FT MUTAGEN 128
FT /note="D->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:25941396"
FT MUTAGEN 131
FT /note="K->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:25941396"
FT MUTAGEN 147
FT /note="K->A: Loss of activity by 90%."
FT /evidence="ECO:0000269|PubMed:25941396"
FT CONFLICT 17
FT /note="D -> N (in Ref. 1; CAA49863)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..97
FT /note="PEHNRV -> RAQSG (in Ref. 1; CAA49863)"
FT /evidence="ECO:0000305"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1EKS"
FT STRAND 24..35
FT /evidence="ECO:0007829|PDB:4PYA"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:4PYA"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:4PYA"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1EKS"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:4PYA"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:4PYA"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:4PYA"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4PYA"
FT STRAND 96..109
FT /evidence="ECO:0007829|PDB:4PYA"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:4PYA"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:4PYA"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:4PYA"
SQ SEQUENCE 161 AA; 17467 MW; 280DAC1EFAAA04AD CRC64;
MSQLTHINAA GEAHMVDVSA KAETVREARA EAFVTMRSET LAMIIDGRHH KGDVFATARI
AGIQAAKRTW DLIPLCHPLM LSKVEVNLQA EPEHNRVRIE TLCRLTGKTG VEMEALTAAS
VAALTIYDMC KAVQKDMVIG PVRLLAKSGG KSGDFKVEAD D
