Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup BATS domain containing

  HydE/PylB-like

  ⌊ FunctionalDomain uncharacterized HydE/PylB-like sequence (ID 1980375)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Thermotoga maritima MSB8 Taxon ID: 243274 485602200 PRP URP

Uniprot

Protein NameAccessionEC Number Identifier
[FeFe] hydrogenase maturase subunit HydE {ECO:0000305} Q9X0Z6 HYDE_THEMA (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 358 | Length of Functional Domain: 343

1       10        20        30        40        50        60

MWSHPQFEKASTGREILEKLERREFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDE
VHIRAI
IEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFGAKTIVLQSGE
DPYYMPDVISDIVKEIKKMGVAVTLSLGEWPREYYEKWKEAGADRYLLRHETANPVLHRK
LRPDTSFENRLNCLLTLKELGYETGAGSMVGLPGQTIDDLVDDLLF
LKEHDFDMVGIGPF
IPHPDTPLANEKKGDFTLTLKMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVI
MPNWTPSPYRQLYQLYPGKICVFEKDTACIPCVMKMIELLGRKPGRDWGGRKRVFET
V
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
73 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
77 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
80 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
73 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
77 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
80 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Links
4JY8 X-Ray Snapshots Of Possible Intermediates In The Time Course Of Synthesis And Degradation Of Protein-Bound Fe4S4 Clusters Fefe-Hydrogenase Maturase 10 2.9 Iron/Sulfur Cluster
(3 more ⇓)
CSA • PDB • PDBSum
4JY9 X-Ray Snapshots Of Possible Intermediates In The Time Course Of Synthesis And Degradation Of Protein-Bound Fe4S4 Clusters Fefe-Hydrogenase Maturase 10 1.6 Iron/Sulfur Cluster
(4 more ⇓)
CSA • PDB • PDBSum
4JXC X-Ray Snapshots Of Possible Intermediates In The Time Course Of Synthesis And Degradation Of Protein-Bound Fe4S4 Clusters Fefe-Hydrogenase Maturase 9 1.5 S-Hydroxycysteine
(9 more ⇓)
CSA • PDB • PDBSum
3CIX X-Ray Structure Of The [Fefe]-Hydrogenase Maturase Hyde From Thermotoga Maritima In Complex With Thiocyanate Fefe-Hydrogenase Maturase 9 1.7 S-Hydroxycysteine
(9 more ⇓)
CSA • PDB • PDBSum
3IIZ X-Ray Structure Of The Fefe-Hydrogenase Maturase Hyde From T. Maritima In Complex With S-Adenosyl-L-Methionine Biotin Synthetase, Putative 9 1.62 2-Amino-3-(4-Hydroxy-6-Oxocyclohexa-1,4-Dienyl) Propanoic Acid
(8 more ⇓)
CSA • PDB • PDBSum
4JYE X-Ray Snapshots Of Possible Intermediates In The Time Course Of Synthesis And Degradation Of Protein-Bound Fe4S4 Clusters. Biotin Synthetase, Putative 9 1.65 2-Hydroxy-L-Tyrosine
(6 more ⇓)
CSA • PDB • PDBSum
4JYD X-Ray Snapshots Of Possible Intermediates In The Time Course Of Synthesis And Degradation Of Protein-Bound Fe4S4 Clusters. Fefe-Hydrogenase Maturase 9 1.71 2-Hydroxy-L-Tyrosine
(7 more ⇓)
CSA • PDB • PDBSum
4JYF X-Ray Snapshots Of Possible Intermediates In The Time Course Of Synthesis And Degradation Of Protein-Bound Fe4S4 Clusters. Fefe-Hydrogenase Maturase 9 1.45 2-Hydroxy-L-Tyrosine
(7 more ⇓)
CSA • PDB • PDBSum
3IIX X-Ray Structure Of The Fefe-Hydrogenase Maturase Hyde From T. Maritima In Complex With Methionine And 5'Deoxyadenosine Biotin Synthetase, Putative 9 1.25 2-Amino-3-(4-Hydroxy-6-Oxocyclohexa-1,4-Dienyl) Propanoic Acid
(8 more ⇓)
CSA • PDB • PDBSum
3CIW X-Ray Structure Of The [Fefe]-Hydrogenase Maturase Hyde From Thermotoga Maritima Fefe-Hydrogenase Maturase 9 1.35 2-Amino-3-(4-Hydroxy-6-Oxocyclohexa-1,4-Dienyl) Propanoic Acid
(6 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, 4:03 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
update domain start position 3 4
Sept. 15, 2014, 3:39 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update name HydE uncharacterized HydE protein
update domain start position 4 14
update subgroup - BATS domain containing
May 11, 2015, 8:57 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
remove family assignment evidence code IEA -
remove family [FeFe] hydrogenase maturase (HydE-like) -
Dec. 17, 2015, 4:12 a.m. update curation agent setDomainBoundaries.py holliday
update name uncharacterized HydE protein uncharacterized HydE/PylB-like sequence
update subgroup BATS domain containing HydE/PylB-like
Oct. 15, 2016, 3:57 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 358 357
update domain start position 14 15
EC number assigned by UniProtKB accession ID.