MOAC2_MYCTU
ID MOAC2_MYCTU Reviewed; 167 AA.
AC P9WJR7; L0T7Y3; O53876; P0A5K6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Cyclic pyranopterin monophosphate synthase 2 {ECO:0000255|HAMAP-Rule:MF_01224};
DE EC=4.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01224};
DE AltName: Full=Molybdenum cofactor biosynthesis protein C 2 {ECO:0000255|HAMAP-Rule:MF_01224};
GN Name=moaC2; OrderedLocusNames=Rv0864; ORFNames=MTV043.57;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP CRYSTALLIZATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22684071; DOI=10.1107/s174430911201665x;
RA Srivastava S., Srivastava V.K., Arora A., Pratap J.V.;
RT "Overexpression, purification, crystallization and preliminary X-ray
RT analysis of putative molybdenum cofactor biosynthesis protein C (MoaC2)
RT from Mycobacterium tuberculosis H37Rv.";
RL Acta Crystallogr. F 68:687-691(2012).
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}.
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000255|HAMAP-
CC Rule:MF_01224}.
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DR EMBL; AL123456; CCP43612.1; -; Genomic_DNA.
DR PIR; H70815; H70815.
DR RefSeq; NP_215379.1; NC_000962.3.
DR RefSeq; WP_003404544.1; NZ_NVQJ01000040.1.
DR PDB; 4FDF; X-ray; 2.20 A; A/B=1-167.
DR PDBsum; 4FDF; -.
DR AlphaFoldDB; P9WJR7; -.
DR SMR; P9WJR7; -.
DR STRING; 83332.Rv0864; -.
DR PaxDb; P9WJR7; -.
DR DNASU; 885826; -.
DR GeneID; 885826; -.
DR KEGG; mtu:Rv0864; -.
DR TubercuList; Rv0864; -.
DR eggNOG; COG0315; Bacteria.
DR OMA; IWDMVKS; -.
DR PhylomeDB; P9WJR7; -.
DR BRENDA; 4.6.1.17; 3445.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
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; Lyase; Molybdenum cofactor biosynthesis; Reference proteome.
FT CHAIN 1..167
FT /note="Cyclic pyranopterin monophosphate synthase 2"
FT /id="PRO_0000097812"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 86..88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 122..123
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:4FDF"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:4FDF"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:4FDF"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:4FDF"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:4FDF"
FT STRAND 103..118
FT /evidence="ECO:0007829|PDB:4FDF"
FT HELIX 121..139
FT /evidence="ECO:0007829|PDB:4FDF"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:4FDF"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:4FDF"
SQ SEQUENCE 167 AA; 17598 MW; 07216D9B18C05E90 CRC64;
MARASGASDY RSGELSHQDE RGAAHMVDIT EKATTKRTAV AAGILRTSAQ VVALISTGGL
PKGDALATAR VAGIMAAKRT SDLIPLCHQL ALTGVDVDFT VGQLDIEITA TVRSTDRTGV
EMEALTAVSV AALTLYDMIK AVDPGALIDD IRVLHKEGGR RGTWTRR
