ID A0A0N5CEU4_STREA Unreviewed; 333 AA.
AC A0A0N5CEU4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE RecName: Full=Molybdopterin synthase catalytic subunit {ECO:0000256|HAMAP-Rule:MF_03052};
DE EC=2.8.1.12 {ECO:0000256|HAMAP-Rule:MF_03052};
DE AltName: Full=Molybdenum cofactor synthesis protein 2 large subunit {ECO:0000256|HAMAP-Rule:MF_03052};
DE AltName: Full=Molybdenum cofactor synthesis protein 2B {ECO:0000256|HAMAP-Rule:MF_03052};
DE Short=MOCS2B {ECO:0000256|HAMAP-Rule:MF_03052};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001638100.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001638100.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a
CC complex that catalyzes the conversion of precursor Z into
CC molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms
CC from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene
CC group. {ECO:0000256|HAMAP-Rule:MF_03052}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03052};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03052}.
CC -!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
CC (MOCS2B) subunits. {ECO:0000256|HAMAP-Rule:MF_03052}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03052}.
CC -!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03052}.
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DR AlphaFoldDB; A0A0N5CEU4; -.
DR STRING; 174720.A0A0N5CEU4; -.
DR WBParaSite; SPAL_0001638100.1; SPAL_0001638100.1; SPAL_0001638100.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000046392; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00756; MoaE; 1.
DR Gene3D; 3.90.1170.40; Molybdopterin biosynthesis MoaE subunit; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03052; MOC2B; 1.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR028888; MOCS2B_euk.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23404:SF2; MOLYBDOPTERIN SYNTHASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR23404; MOLYBDOPTERIN SYNTHASE RELATED; 1.
DR Pfam; PF02391; MoaE; 1.
DR SUPFAM; SSF54690; Molybdopterin synthase subunit MoaE; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03052};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_03052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03052}.
FT BINDING 292..293
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03052"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03052"
FT BINDING 315..317
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03052"
SQ SEQUENCE 333 AA; 38525 MW; B49A0625F1550829 CRC64;
MVFILGISGC TCSGKTTLSN ILFKKALEKK IKVDKISQDD FYLNKEEVRQ IKNKENSDIV
FYDYDSVSAL DKKKIINEVN LKKQNCDLLI IEGTMLLEIE EIISSLSKIF YITLEKDICG
ERRKNRKDYD PPDNVGYFDQ IVWPSYENNL KIAKNLSNLY GKNFISFVDG KDICLDQINN
FCDHLWREIK LDVVRIVIDD EIDINQITKI ITSPSCGAIS IFIGTTRDNF DGKEVIRLEY
ECYEEMALKE MKKLCIKGRD KYKTIQNIAI FHRVEHVPVT EASVVIAVSS PHRHECQEAT
SFLIDQLKVT VPIWKKEIYS DNSGQWKRNC CKS
//
