ID   MOAE_BRUME              Reviewed;         163 AA.
AC   P65396; Q8YGA6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=BMEI1254;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(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; AE008917; AAL52435.1; -; Genomic_DNA.
DR   PIR; AH3408; AH3408.
DR   RefSeq; WP_002963838.1; NZ_GG703778.1.
DR   AlphaFoldDB; P65396; -.
DR   SMR; P65396; -.
DR   STRING; 224914.BMEI1254; -.
DR   EnsemblBacteria; AAL52435; AAL52435; BMEI1254.
DR   GeneID; 45051776; -.
DR   GeneID; 55590418; -.
DR   KEGG; bme:BMEI1254; -.
DR   PATRIC; fig|224914.52.peg.157; -.
DR   eggNOG; COG0314; Bacteria.
DR   OMA; WPLQRVS; -.
DR   PhylomeDB; P65396; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000419; Chromosome I.
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..163
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000163079"
FT   REGION          138..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         107..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   163 AA;  18396 MW;  B622143ED5116118 CRC64;
     MDGQPTCPLS ISVRSEDFDI AAEIDRIGKN RREIGAIVTF TGLCRDEDGQ LAALELEHYP
     GMAQAEISRM AKQALERWPL NGLTIIHRYG LIKPGENIVL VVAASRHRHA AFEAASFLMD
     YMKTNAPFWK REHLADGTAG GWVSSKEEDE ESRKRWEEPR KSE