MOAE_NOSS1
ID MOAE_NOSS1 Reviewed; 165 AA.
AC Q8YWH5;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=all1638;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(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; BA000019; BAB78004.1; -; Genomic_DNA.
DR PIR; AH2010; AH2010.
DR RefSeq; WP_010995807.1; NZ_RSCN01000013.1.
DR AlphaFoldDB; Q8YWH5; -.
DR SMR; Q8YWH5; -.
DR STRING; 103690.17135458; -.
DR EnsemblBacteria; BAB78004; BAB78004; BAB78004.
DR KEGG; ana:all1638; -.
DR eggNOG; COG0314; Bacteria.
DR OMA; WPLQRVS; -.
DR OrthoDB; 1877633at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000002483; 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..165
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000163075"
FT BINDING 51..53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 118..119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141..143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 165 AA; 18098 MW; 44A5B5A6654CA40E CRC64;
MKSVLPSTPI VTLKPKIEDS FAITFAPLSL EEIHALADDS ANGAVVVMSG MVRNQTDGKP
VVSLEYQAYE PMALRVFYQI AADIRSAWPA VNRVVIHHRI GRLQVGQISV LVAIGCPHRS
EAFAACRYAI DTLKHNAPIW KKEHWQDGSS TWVSIGACEQ SGQNC
