MOAE2_MYCTO
ID MOAE2_MYCTO Reviewed; 141 AA.
AC P9WJR0; L0T6N7; O53878;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Molybdopterin synthase catalytic subunit 2;
DE EC=2.8.1.12;
DE AltName: Full=MPT synthase subunit 2 2;
DE AltName: Full=Molybdenum cofactor biosynthesis protein E 2;
DE AltName: Full=Molybdopterin-converting factor large subunit 2;
DE AltName: Full=Molybdopterin-converting factor subunit 2 2;
GN Name=moaE2; OrderedLocusNames=MT0889;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK45130.1; -; Genomic_DNA.
DR PIR; B70816; B70816.
DR RefSeq; WP_003404552.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJR0; -.
DR SMR; P9WJR0; -.
DR EnsemblBacteria; AAK45130; AAK45130; MT0889.
DR GeneID; 45424832; -.
DR KEGG; mtc:MT0889; -.
DR PATRIC; fig|83331.31.peg.954; -.
DR HOGENOM; CLU_089568_1_1_11; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis; Transferase.
FT CHAIN 1..141
FT /note="Molybdopterin synthase catalytic subunit 2"
FT /id="PRO_0000427786"
FT BINDING 37..39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103..104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 126..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 141 AA; 15048 MW; 5FEB28B7EA1FB62B CRC64;
MTQVLRAALT DQPIFLAEHE ELVSHRSAGA IVGFVGMIRD RDGGRGVLRL EYSAHPSAAQ
VLADLVAEVA EESSGVRAVA ASHRIGVLQV GEAALVAAVA ADHRRAAFGT CAHLVETIKA
RLPVWKHQFF EDGTDEWVGS V