MOAC1_MYCTU
ID MOAC1_MYCTU Reviewed; 170 AA.
AC P9WJR9; L0TBK8; O05788; P0A5K4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Cyclic pyranopterin monophosphate synthase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01224};
GN Name=moaC1; Synonyms=moaC; OrderedLocusNames=Rv3111; ORFNames=MTCY164.21;
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 INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20378651; DOI=10.1099/mic.0.037200-0;
RA Mendoza Lopez P., Golby P., Wooff E., Nunez Garcia J., Garcia Pelayo M.C.,
RA Conlon K., Gema Camacho A., Hewinson R.G., Polaina J., Suarez Garcia A.,
RA Gordon S.V.;
RT "Characterization of the transcriptional regulator Rv3124 of Mycobacterium
RT tuberculosis identifies it as a positive regulator of molybdopterin
RT biosynthesis and defines the functional consequences of a non-synonymous
RT SNP in the Mycobacterium bovis BCG orthologue.";
RL Microbiology 156:2112-2123(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Beijing GC1237;
RX PubMed=20844580; DOI=10.1371/journal.ppat.1001100;
RA Brodin P., Poquet Y., Levillain F., Peguillet I., Larrouy-Maumus G.,
RA Gilleron M., Ewann F., Christophe T., Fenistein D., Jang J., Jang M.S.,
RA Park S.J., Rauzier J., Carralot J.P., Shrimpton R., Genovesio A.,
RA Gonzalo-Asensio J.A., Puzo G., Martin C., Brosch R., Stewart G.R.,
RA Gicquel B., Neyrolles O.;
RT "High content phenotypic cell-based visual screen identifies Mycobacterium
RT tuberculosis acyltrehalose-containing glycolipids involved in phagosome
RT remodeling.";
RL PLoS Pathog. 6:E1001100-E1001100(2010).
CC -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC (cPMP) (By similarity). Probably plays a role in host phagosome
CC maturation arrest (PubMed:20844580). {ECO:0000255|HAMAP-Rule:MF_01224,
CC ECO:0000305|PubMed:20844580}.
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 -!- INDUCTION: Expression is positively regulated by the transcriptional
CC regulator MoaR1. {ECO:0000269|PubMed:20378651}.
CC -!- DISRUPTION PHENOTYPE: Grows normally in liquid culture, traffics into
CC host (human and mouse) acidified compartments early after phagocytosis,
CC suggesting it no longer arrests phagosome maturation as well as wild-
CC type, impaired growth in mouse macrophages (PubMed:20844580).
CC {ECO:0000269|PubMed:20844580}.
CC -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000255|HAMAP-
CC Rule:MF_01224}.
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DR EMBL; AL123456; CCP45921.1; -; Genomic_DNA.
DR PIR; F70920; F70920.
DR RefSeq; WP_003899917.1; NZ_NVQJ01000011.1.
DR RefSeq; YP_177927.1; NC_000962.3.
DR AlphaFoldDB; P9WJR9; -.
DR SMR; P9WJR9; -.
DR STRING; 83332.Rv3111; -.
DR PaxDb; P9WJR9; -.
DR DNASU; 888680; -.
DR GeneID; 888680; -.
DR KEGG; mtu:Rv3111; -.
DR TubercuList; Rv3111; -.
DR eggNOG; COG0315; Bacteria.
DR OMA; EASCTGK; -.
DR PhylomeDB; P9WJR9; -.
DR UniPathway; UPA00344; -.
DR PHI-base; PHI:7748; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
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 GO; GO:0052170; P:suppression by symbiont of host innate immune response; IDA:MTBBASE.
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 2: Evidence at transcript level;
KW Lyase; Molybdenum cofactor biosynthesis; Reference proteome.
FT CHAIN 1..170
FT /note="Cyclic pyranopterin monophosphate synthase 1"
FT /id="PRO_0000097810"
FT ACT_SITE 131
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 79..81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ SEQUENCE 170 AA; 17845 MW; BA135681145FE414 CRC64;
MIDHALALTH IDERGAARMV DVSEKPVTLR VAKASGLVIM KPSTLRMISD GAAAKGDVMA
AARIAGIAAA KRTGDLIPLC HPLGLDAVSV TITPCEPDRV KILATTTTLG RTGVEMEALT
AVSVAALTIY DMCKAVDRAM EISQIVLQEK SGGRSGVYRR SASDLACQSR
