MOAE_PASMU
ID MOAE_PASMU Reviewed; 150 AA.
AC Q9CN24;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Molybdopterin synthase catalytic subunit;
DE EC=2.8.1.12;
DE AltName: Full=MPT synthase subunit 2;
DE AltName: Full=Molybdenum cofactor biosynthesis protein E;
DE AltName: Full=Molybdopterin-converting factor large subunit;
DE AltName: Full=Molybdopterin-converting factor subunit 2;
GN Name=moaE; OrderedLocusNames=PM0622;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02706.1; -; Genomic_DNA.
DR RefSeq; WP_005751475.1; NC_002663.1.
DR AlphaFoldDB; Q9CN24; -.
DR SMR; Q9CN24; -.
DR STRING; 747.DR93_1452; -.
DR EnsemblBacteria; AAK02706; AAK02706; PM0622.
DR KEGG; pmu:PM0622; -.
DR PATRIC; fig|272843.6.peg.630; -.
DR HOGENOM; CLU_089568_2_1_6; -.
DR OMA; WPLQRVS; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000809; 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; Reference proteome; Transferase.
FT CHAIN 1..150
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000163089"
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 150 AA; 17156 MW; 896F637B55507E95 CRC64;
MSDIQIAVQE QPFDQNAAYR WLSEQHSVGA TVVFVGKVRD LNLGDEVSSL YLEHYPAMTE
KALTEIVAQA KARWDIQRVC VIHRVGLLQT GDEIVFVGVS SAHRGEAYQA NEFIMDFLKS
KAPFWKKEKT TQGERWIESR DTDQQALARW