Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup SPASM/twitch domain containing

  ⌊ main SPASM domain-containing

  ⌊ cyclic pyranopterin phosphate synthase (MoaA-like)

     ⌊ Family cyclic pyranopterin phosphate synthase (MoaA-like)

  ⌊ FunctionalDomain Molybdenum cofactor biosynthesis protein (ID 2019764)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code ISS
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Staphylococcus aureus Taxon ID: 1280 686323513 WP_031876894.1 (RefSeq) URP
Staphylococcus aureus M1151 Taxon ID: 1402663 586260541 EWQ64818.1 (Genbank) URP

Sequence

Length of Enzyme (full-length): 326 | Length of Functional Domain: 326

1       10        20        30        40        50        60

MVEQIKDKLGRPIRDLRLSVTDRCNFRCDYCMPKEVFGDDFVFLPKNELLTFDEMARIAK
VYAELGVKKIRITGGEPLMRRDLDVLIAKLNQIDGIEDIGLTTNGLLLKKHGQKLYDAGL
RRINVSLDAIDDTLFQSINNRNIKATTILEQIDYATSIGLNVKVNVVIQKGINDDQIIPM
LEYFKDKHIEIRFIEFMDVGNDNGWDFSKVVTKDEMLTMIEQHFEINPVEPKYFGEVAKY
YRHKDNGVQFGLITSVSQSFCSTCTRARLSSDGKFYGCLFATVDGFNVKTFIRSGVTDEE
LKEQFKALWQIRDDRYSDERTAQTVA
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
24 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
28 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
31 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 7/7 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
24 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
28 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
31 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
75 Gly (G) side chain Binds S-adensosylmethionine
Notes: Acts via the carbonyl group of the backbone 		substrate binding -- binding ISS
261 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
264 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
278 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 12/12 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
24 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
28 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
30 Tyr (Y) side chain Binds S-adensosylmethionine substrate binding -- binding ICS PubMed:16632608
31 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
71 Arg (R) side chain Binds GTP substrate binding -- binding ISS
75 Gly (G) side chain Binds S-adensosylmethionine
Notes: Acts via the carbonyl group of the backbone 		substrate binding -- binding ICS PubMed:16632608
126 Ser (S) side chain Binds S-adensosylmethionine substrate binding -- binding ICS PubMed:16632608
163 Lys (K) side chain Binds GTP substrate binding -- binding ISS
197 Met (M) side chain Binds S-adensosylmethionine
Notes: Acts via both the amide and carbonyl groups of the backbone. 		substrate binding -- binding ICS PubMed:16632608
261 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
264 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
278 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2FB3 Structure Of Moaa In Complex With 5'-Gtp Molybdenum Cofactor Biosynthesis Protein A 49 2.35 Sulfate Ion
(5 more ⇓) 		CSA • PDB • PDBSum
1TV8 Structure Of Moaa In Complex With S-Adenosylmethionine Molybdenum Cofactor Biosynthesis Protein A 49 2.2 Sulfate Ion
(3 more ⇓) 		CSA • PDB • PDBSum
1TV7 Structure Of The S-Adenosylmethionine Dependent Enzyme Moaa Molybdenum Cofactor Biosynthesis Protein A 49 2.8 Sulfate Ion • Iron/Sulfur Cluster CSA • PDB • PDBSum
2FB2 Structure Of The Moaa Arg17/266/268/Ala Triple Mutant Molybdenum Cofactor Biosynthesis Protein A 48 2.25 Yes Sulfate Ion
(2 more ⇓) 		CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
July 15, 2014, 4:30 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
update domain end position 325 326
Oct. 15, 2016, 4:24 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update family assignment evidence code IEA ISS
update name Molybdenum cofactor biosynthesis protein A (MoaA) Molybdenum cofactor biosynthesis protein
update subgroup SPASM/twitch domain containing cyclic pyranopterin phosphate synthase (MoaA-like)
update superfamily assignment evidence code IEA ISS
EC number assigned by UniProtKB accession ID.