ID M8E9G6_9BACL Unreviewed; 235 AA.
AC M8E9G6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=I532_14718 {ECO:0000313|EMBL:EMT52105.1};
OS Brevibacillus borstelensis AK1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT52105.1, ECO:0000313|Proteomes:UP000012081};
RN [1] {ECO:0000313|EMBL:EMT52105.1, ECO:0000313|Proteomes:UP000012081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT52105.1,
RC ECO:0000313|Proteomes:UP000012081};
RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA Sivakumar N.;
RT "Assembly of a new bacterial strain Brevibacillus borstelensis AK1.";
RL Submitted (MAR-2013) 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}.
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:EMT52105.1}.
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DR EMBL; APBN01000005; EMT52105.1; -; Genomic_DNA.
DR RefSeq; WP_003389141.1; NZ_APBN01000005.1.
DR AlphaFoldDB; M8E9G6; -.
DR STRING; 1300222.I532_14718; -.
DR GeneID; 72736035; -.
DR PATRIC; fig|1300222.3.peg.3077; -.
DR OrthoDB; 9803224at2; -.
DR Proteomes; UP000012081; 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 NCBIfam; TIGR01682; moaD; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000012081}.
FT REGION 214..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 235 AA; 25631 MW; 44B11AE4EBF3726C CRC64;
MQISVLLFAG LAELAGERTI QLTLPEGATV QDLLQAASSQ YPALSSLLGS CFISVNQEYA
KPDTAIRAGD EIAILPPVSG GQDPRFAITT EPLSADKLVK LVSNPHAGAV LAFVGTVREF
THGQRTVLLA YEAYEPMAVE KMKQIASEVE ERWPGTKLAM HHRIGELAIE EIAVVAAVAT
PHRKAAFEAG EYAIERLKQI VPIWKKEIWE DGSEWKGHQQ GPWNPTALPD DVERS
//
