MOAE_AQUAE
ID MOAE_AQUAE Reviewed; 154 AA.
AC O67928;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=aq_2181;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of molybdopterin converting factor subunit 2 (aq_2181)
RT from Aquifex aeolicus VF5.";
RL Submitted (FEB-2009) to the PDB data bank.
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}.
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; AE000657; AAC07878.1; -; Genomic_DNA.
DR PIR; D70487; D70487.
DR RefSeq; NP_214497.1; NC_000918.1.
DR RefSeq; WP_010881433.1; NC_000918.1.
DR PDB; 2OMD; X-ray; 2.00 A; A/B=1-154.
DR PDBsum; 2OMD; -.
DR AlphaFoldDB; O67928; -.
DR SMR; O67928; -.
DR STRING; 224324.aq_2181; -.
DR EnsemblBacteria; AAC07878; AAC07878; aq_2181.
DR KEGG; aae:aq_2181; -.
DR PATRIC; fig|224324.8.peg.1687; -.
DR eggNOG; COG0314; Bacteria.
DR HOGENOM; CLU_089568_1_2_0; -.
DR InParanoid; O67928; -.
DR OMA; GEICLFV; -.
DR OrthoDB; 1877633at2; -.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; O67928; -.
DR Proteomes; UP000000798; 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 1: Evidence at protein level;
KW 3D-structure; Molybdenum cofactor biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..154
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000163076"
FT BINDING 40..42
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107..108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 130..132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:2OMD"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:2OMD"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2OMD"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2OMD"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:2OMD"
FT HELIX 60..78
FT /evidence="ECO:0007829|PDB:2OMD"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:2OMD"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:2OMD"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:2OMD"
FT HELIX 108..125
FT /evidence="ECO:0007829|PDB:2OMD"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:2OMD"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2OMD"
SQ SEQUENCE 154 AA; 17579 MW; 84BDCBD4FD54DF34 CRC64;
MEVGMIPRVY LGHEWFGAER ILSEYQVPED CGAQVLFLGI PRNAPEDGGN IEALEYEAYP
EMAIKEMEKI RQETIEKFGV KEVFIHHRLG LVKIGEPSFL VLAVGGHREE TFKACRYAVD
ETKKRVPIWK KEIFKEGKGE WVLGEKKNAS GQTK
