ID A0A1I4NWZ5_9BACL Unreviewed; 232 AA.
AC A0A1I4NWZ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=Molybdopterin synthase catalytic subunit {ECO:0000256|ARBA:ARBA00013858};
DE EC=2.8.1.12 {ECO:0000256|ARBA:ARBA00011950};
DE AltName: Full=MPT synthase subunit 2 {ECO:0000256|ARBA:ARBA00030781};
DE AltName: Full=Molybdenum cofactor biosynthesis protein E {ECO:0000256|ARBA:ARBA00029745};
DE AltName: Full=Molybdopterin-converting factor large subunit {ECO:0000256|ARBA:ARBA00030407};
DE AltName: Full=Molybdopterin-converting factor subunit 2 {ECO:0000256|ARBA:ARBA00032474};
GN ORFNames=SAMN03159341_12023 {ECO:0000313|EMBL:SFM19850.1};
OS Paenibacillus sp. 1_12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566278 {ECO:0000313|EMBL:SFM19850.1, ECO:0000313|Proteomes:UP000198699};
RN [1] {ECO:0000313|EMBL:SFM19850.1, ECO:0000313|Proteomes:UP000198699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_12 {ECO:0000313|EMBL:SFM19850.1,
RC ECO:0000313|Proteomes:UP000198699};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000676};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
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. {ECO:0000256|ARBA:ARBA00026066}.
CC -!- SIMILARITY: Belongs to the MoaE family.
CC {ECO:0000256|ARBA:ARBA00005426}.
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DR EMBL; FOTE01000020; SFM19850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4NWZ5; -.
DR STRING; 1566278.SAMN03159341_12023; -.
DR Proteomes; UP000198699; Unassembled WGS sequence.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:InterPro.
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 InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR036563; MoaE_sf.
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;
SQ SEQUENCE 232 AA; 26244 MW; 75B0BC80FE74B228 CRC64;
MMKFNIQVFA GLAERMQGPL FVLDWDSSIP LTPVILKEHL QVQYPEASTL LSQAFVAINQ
SYAGDHQIIH ENDEIAIIPP VSGGQPKRAE LTREKISIEQ VTAQVLHPNH GAALTFIGTT
REWTHGKRTT MLEYEAYEPM AVKMMEQIVA FIHDQYEGAL CAITHRLGKV DIGEISVVIA
VSAPHRDAAY EANRYAIERL KQVVPIWKKE IWEDGSEWKG HQQGPWNPRE VL
//
