Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup SPASM/twitch domain containing

  ⌊ main SPASM domain-containing

  ⌊ thioether bond formation requiring two auxiliary iron-sulfur clusters

     ⌊ Family quinohemoprotein amine dehydrogenase maturation protein (QhpD-like)

  ⌊ FunctionalDomain quinohemoprotein amine dehydrogenase maturation protein QhpD (ID 410011)

Superfamily Assignment Evidence Code(s) ISS PubMed:25778402
Family Assignment Evidence Code CFM PubMed:25778402
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Paracoccus denitrificans Taxon ID: 266 500071986 WP_011747999.1 (RefSeq)
Paracoccus denitrificans PD1222 Taxon ID: 318586 119374208 ABL69801.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a A1B2Q7 A1B2Q7_PARDP (TrEMBL)

Sequence

Length of Enzyme (full-length): 485 | Length of Functional Domain: 481

1       10        20        30        40        50        60

MGALTLIRHNAHRVDVDGHAMLMHVPTTSLFELDGVARDVYDLFRRAPAVDPDLMRAELG
PRHGPDTLSECLQSFLALDILRNAEAADIPRPVVKVEEIPLSTIILNVNTGCNLACTYCY
KEDLTTPAKGQKMGFETAKASFELLLKQAHARDRVNVVFFGGEPLSNMPLIRELVAYARP
RAAELGKAVDFSLTTNATLLTPELVDWFDAHRFALTVSMDGPKALHDANRKTVGGKGTYD
LVARNVRMLLSRYRSRPVGGRVTLTRGVTDVIGIHDHLKNELGFHEVGFGPATSGPIAVF
NLDAEALKRAFEDMKTLGRRYVEAACRGENIGFSNMHQLLTDIAQGTKKAVPCGAGLGML
AVDKDGELHLCHRFVGSNQPTYGNVAKGIDIPKLAGFIETAQDRSAYGCKTCRIRSICAG
GCYHESYARQGDPFAPVWHYCDLMRDWVDFGIESYVRIMQANPSFFRSQLEPRIARSGTA
REVLQ
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
112 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
116 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
119 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 3/3 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
112 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
116 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
119 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 10/10 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
112 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
116 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
119 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
353 Cys (C) side chain Binds auxillary 4Fe-4S cluster metal ligand -- binding IME PubMed:25778402
371 Cys (C) side chain Binds auxillary 4Fe-4S cluster metal ligand -- binding IME PubMed:25778402
409 Cys (C) side chain Binds auxillary 4Fe-4S cluster metal ligand -- binding ISS PubMed:25778402
412 Cys (C) side chain Binds auxillary 4Fe-4S cluster metal ligand -- binding ISS PubMed:25778402
418 Cys (C) side chain Binds auxillary 4Fe-4S cluster metal ligand -- binding ISS PubMed:25778402
422 Cys (C) side chain Binds auxillary 4Fe-4S cluster metal ligand -- binding IME PubMed:25778402
441 Cys (C) side chain Binds auxillary 4Fe-4S cluster metal ligand -- binding ISS PubMed:25778402

Catalyzed Reactions

thioether cross-link between Cys and Asp

+
cysteine residue
32460		 L-aspartic acid residue
29958		 cysteine-aspartyl residue
86402

EC: | IntEnz: | Kegg: | BioCyc: | BRENDA: |

thioether cross-link between Cys and Glu

+ + + +
L-cysteine residue
29950		 glutamate residue
32484		 S-adenosyl-L-methionine zwitterion
59789		 Cys-Glu thioether
132408		 5'-deoxyadenosine
17319		 L-methionine zwitterion
57844

EC: | IntEnz: | Kegg: | BioCyc: | BRENDA: |

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 2:56 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 435 482
update domain start position 78 2
April 9, 2015, 10:15 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update family assignment evidence code IEA CFM
update name Quinohemoprotein amine dehydrogenase maturation protein quinohemoprotein amine dehydrogenase maturation protein QphD
Dec. 17, 2015, 5:37 a.m. update curation agent setDomainBoundaries.py holliday
update name quinohemoprotein amine dehydrogenase maturation protein QphD quinohemoprotein amine dehydrogenase maturation protein QhpD
Jan. 18, 2016, 5:30 a.m. update curation agent holliday setDomainBoundaries.py
Oct. 15, 2016, 6:04 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update subgroup dehydrogenase like thioether bond formation requiring two auxiliary iron-sulfur clusters
EC number assigned by UniProtKB accession ID.