ID A0A195FRI6_9HYME Unreviewed; 335 AA.
AC A0A195FRI6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 22-FEB-2023, entry version 22.
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};
GN Name=Mocs2 {ECO:0000256|HAMAP-Rule:MF_03052};
GN ORFNames=ALC56_02700 {ECO:0000313|EMBL:KYN42897.1};
OS Trachymyrmex septentrionalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN42897.1, ECO:0000313|Proteomes:UP000078541};
RN [1] {ECO:0000313|EMBL:KYN42897.1, ECO:0000313|Proteomes:UP000078541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN42897.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN42897.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex septentrionalis WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the large subunit (MOCS2A). {ECO:0000256|HAMAP-
CC Rule:MF_03052}.
CC -!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03052}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ981305; KYN42897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195FRI6; -.
DR STRING; 34720.A0A195FRI6; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000078541; Unassembled WGS sequence.
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 CDD; cd00754; Ubl_MoaD; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.90.1170.40; Molybdopterin biosynthesis MoaE subunit; 1.
DR HAMAP; MF_03052; MOC2B; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR028888; MOCS2B_euk.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR003749; ThiS/MoaD-like.
DR PANTHER; PTHR23404:SF2; MOLYBDOPTERIN SYNTHASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR23404; MOLYBDOPTERIN SYNTHASE RELATED; 1.
DR Pfam; PF02391; MoaE; 1.
DR Pfam; PF02597; ThiS; 1.
DR SUPFAM; SSF54285; MoaD/ThiS; 1.
DR SUPFAM; SSF54690; Molybdopterin synthase subunit MoaE; 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 Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03052}.
FT BINDING 193..194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03052"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03052"
FT BINDING 216..218
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03052"
SQ SEQUENCE 335 AA; 38285 MW; FFEDACCC68CE0E0E CRC64;
MDKTEIQATI LFFAKARELV GCKECKLSIQ KKLSSADLFD KIVHAFELES IRNQIILAVN
DEFVVPNSIL ILSENDKIAV IPPLSGGLIM EILKNFVKLQ QEELNIVEIM ELVTFPNCGA
ISNFIGITRD NFENKKVIKL EYEAYESMAL KEMTNICNKI RSQWDVEGIA IYHRIGEVPI
SKASVVIAVS SPHREQSLSA VEYAINALKA SVPIWKKEVY ETGEPQWKQN KECKWINTLK
DEEAQMASNI NEKISNKDVV DQNLVQIRAN SEELNRRIES FIERKRQHVN TVNVQEFCRY
SENNDNENSC ARVDAILIRR KDSRSHIKGN NTNSI
//
