MOAE1_MYCTU
ID MOAE1_MYCTU Reviewed; 147 AA.
AC P9WJR3; L0TED5; O05795;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Molybdopterin synthase catalytic subunit 1;
DE EC=2.8.1.12;
DE AltName: Full=MPT synthase subunit 2 1;
DE AltName: Full=Molybdenum cofactor biosynthesis protein E 1;
DE AltName: Full=Molybdopterin-converting factor large subunit 1;
DE AltName: Full=Molybdopterin-converting factor subunit 2 1;
GN Name=moaE1; Synonyms=moaE; OrderedLocusNames=Rv3119; ORFNames=MTCY164.29;
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).
CC -!- FUNCTION: Converts molybdopterin precursor Z into molybdopterin. This
CC requires the incorporation of two sulfur atoms into precursor Z to
CC generate a dithiolene group. The sulfur is provided by MoaD (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2
CC [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly +
CC 4 H(+) + molybdopterin; Xref=Rhea:RHEA:26333, Rhea:RHEA-COMP:12160,
CC Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58698, ChEBI:CHEBI:59648, ChEBI:CHEBI:90619,
CC ChEBI:CHEBI:90778; EC=2.8.1.12;
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Also
CC stable as homodimer. The enzyme changes between these two forms during
CC catalysis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MoaE family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45929.1; -; Genomic_DNA.
DR PIR; F70921; F70921.
DR RefSeq; WP_003899923.1; NZ_NVQJ01000019.1.
DR RefSeq; YP_177931.1; NC_000962.3.
DR PDB; 2WP4; X-ray; 2.49 A; A/B=1-147.
DR PDBsum; 2WP4; -.
DR AlphaFoldDB; P9WJR3; -.
DR SMR; P9WJR3; -.
DR STRING; 83332.Rv3119; -.
DR PaxDb; P9WJR3; -.
DR DNASU; 888811; -.
DR GeneID; 888811; -.
DR KEGG; mtu:Rv3119; -.
DR TubercuList; Rv3119; -.
DR eggNOG; COG0314; Bacteria.
DR OMA; GEICLFV; -.
DR PhylomeDB; P9WJR3; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:MTBBASE.
DR CDD; cd00756; MoaE; 1.
DR Gene3D; 3.90.1170.40; -; 1.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR Pfam; PF02391; MoaE; 1.
DR SUPFAM; SSF54690; SSF54690; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Molybdenum cofactor biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..147
FT /note="Molybdopterin synthase catalytic subunit 1"
FT /id="PRO_0000163087"
FT BINDING 43..45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109..110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132..134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2WP4"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:2WP4"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:2WP4"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:2WP4"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2WP4"
FT HELIX 62..77
FT /evidence="ECO:0007829|PDB:2WP4"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:2WP4"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2WP4"
FT STRAND 99..109
FT /evidence="ECO:0007829|PDB:2WP4"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:2WP4"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2WP4"
SQ SEQUENCE 147 AA; 15920 MW; 22735F7154C1412A CRC64;
MANVVAEGAY PYCRLTDQPL SVDEVLAAVS GPEQGGIVIF VGNVRDHNAG HDVTRLFYEA
YPPMVIRTLM SIIGRCEDKA EGVRVAVAHR TGELQIGDAA VVIGASAPHR AEAFDAARMC
IELLKQEVPI WKKEFSSTGA EWVGDRP
