MOAE_BACSU
ID MOAE_BACSU Reviewed; 157 AA.
AC O31705;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Molybdopterin synthase catalytic subunit;
DE EC=2.8.1.12;
DE AltName: Full=MPT synthase subunit 2;
DE AltName: Full=Molybdenum cofactor biosynthesis protein E;
DE AltName: Full=Molybdopterin-converting factor large subunit;
DE AltName: Full=Molybdopterin-converting factor subunit 2;
GN Name=moaE; OrderedLocusNames=BSU14300;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Caldwell R.M., Ferrari E.;
RT "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Converts molybdopterin precursor Z into molybdopterin. This
CC requires the incorporation of two sulfur atoms into precursor Z to
CC generate a dithiolene group. The sulfur is provided by MoaD (By
CC similarity). {ECO:0000250}.
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 -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MoaE family. {ECO:0000305}.
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DR EMBL; AF012285; AAC24904.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13303.1; -; Genomic_DNA.
DR PIR; B69659; B69659.
DR RefSeq; NP_389313.1; NC_000964.3.
DR RefSeq; WP_003232367.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31705; -.
DR SMR; O31705; -.
DR STRING; 224308.BSU14300; -.
DR jPOST; O31705; -.
DR PaxDb; O31705; -.
DR PRIDE; O31705; -.
DR EnsemblBacteria; CAB13303; CAB13303; BSU_14300.
DR GeneID; 936092; -.
DR KEGG; bsu:BSU14300; -.
DR PATRIC; fig|224308.179.peg.1560; -.
DR eggNOG; COG0314; Bacteria.
DR InParanoid; O31705; -.
DR OMA; HERKSCC; -.
DR PhylomeDB; O31705; -.
DR BioCyc; BSUB:BSU14300-MON; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00756; MoaE; 1.
DR Gene3D; 3.90.1170.40; -; 1.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR Pfam; PF02391; MoaE; 1.
DR SUPFAM; SSF54690; SSF54690; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..157
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000163078"
FT BINDING 34..36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 100..101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123..125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 157 AA; 17782 MW; DF207E2DA13BEC9E CRC64;
MERFEITKTP INTENIIKKV EKREAGAITT FIGTVREWTN GKRTVRLEYE AYEPMAVQML
AQIGAEIEEK WEGASAAITH RIGVLDIGEA AVVIAVSSPH RKAAYEANEY AIERIKQIVP
IWKKEIWEDG EQWIGDQLET TAYPNGKPDL SEGEQHD
