ID A0A0E9NE43_SAICN Unreviewed; 427 AA.
AC A0A0E9NE43;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 08-NOV-2023, entry version 26.
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 ORFNames=G7K_2306-t1 {ECO:0000313|EMBL:GAO48122.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO48122.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO48122.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO48122.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO48122.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO48122.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO48122.1}.
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DR EMBL; BACD03000013; GAO48122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9NE43; -.
DR STRING; 698492.A0A0E9NE43; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000033140; 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 Gene3D; 3.90.1170.40; Molybdopterin biosynthesis MoaE subunit; 1.
DR Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 2.
DR HAMAP; MF_03052; MOC2B; 1.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR028888; MOCS2B_euk.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR InterPro; IPR011320; RNase_H1_N.
DR InterPro; IPR037056; RNase_H1_N_sf.
DR PANTHER; PTHR23404:SF2; MOLYBDOPTERIN SYNTHASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR23404; MOLYBDOPTERIN SYNTHASE RELATED; 1.
DR Pfam; PF01693; Cauli_VI; 2.
DR Pfam; PF02391; MoaE; 1.
DR SUPFAM; SSF55658; L9 N-domain-like; 2.
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:UP000033140};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03052}.
FT DOMAIN 5..47
FT /note="Ribonuclease H1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01693"
FT DOMAIN 113..155
FT /note="Ribonuclease H1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01693"
FT REGION 178..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 317..318
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03052"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03052"
FT BINDING 340..342
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03052"
SQ SEQUENCE 427 AA; 47771 MW; F7B8775E6C54485A CRC64;
MPIQYYAVAI GRKPGLYHDW DACDAQVSGY PGARYRAFTD RSEAEEFVLT VNPGAEHNLT
VGDFQRPWLD RRNSDLPPTP APAAPPVTQI VVTNADADAE KDASAKAYAP KAYYAVAVGR
RPGVYYDWPT CSAQVTGYPG ARYKSFQDRN EAEEFVLTLN PGAEEEMLLN DLQRPYLDRR
SSNLPPLPTP AQAQPQSEKE EPKGGEQRTW IAETGDERLF VSLTYDTLDV KTQIDRVRSP
KAGAIVLFSG TTRDNFENKP VTHLSYESYT PLALTSLTHI ATTALQRWNL EGVAVTHRLG
TVGVGEESIL IAVSCGHRKE SFEAGEWVLE EVKKRAEVWK REEYGVVGEG AKWKENFEGA
RPGPERSSFV AANVNANSRL EIILDVWSSV EVILHPWDFA SLYLQATLDL CLRRRSTQYL
NRKDFTP
//
