Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup BATS domain containing

  ⌊ HydE/PylB-like

  ⌊ FunctionalDomain uncharacterized HydE/PylB-like sequence (ID 419383)

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 485602204 PRP URP
Thermotoga maritima Taxon ID: 2336 259090312 URP
Thermotoga maritima Taxon ID: 2336 178847575 URP

Uniprot

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

Sequence

Length of Enzyme (full-length): 348 | Length of Functional Domain: 343

1       10        20        30        40        50        60

MTGREILEKLERREFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDEVHIRAIIEFS
NVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFGAKTIVLQSGEDPYXMPDVIS
DIVKEIKKMGVAVTLSLGEWPREYYEKWKEAGADRYLLRHETANPVLHRKLRPDTSFENR
LNXLLTLKELGYETGAGSMVGLPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLAN
EKKGDFTLTLKMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMPNWTPSPYR
QLYQLYPGKICVFEKDTACIPXVMKMIELLGRKPGRDWGGRKRVFETV
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
63 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
67 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
70 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
63 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
67 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
70 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
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
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
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
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
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
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
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
5FF3 Hyde From T. Maritima In Complex With 4R-Tca [Fefe] Hydrogenase Maturase Subunit Hyde 6 1.18 2-Hydroxy-L-Tyrosine
(7 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
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
5FF2 Hyde From T. Maritima In Complex With (2R,4R)-Tda [Fefe] Hydrogenase Maturase Subunit Hyde 7 1.47 Iron/Sulfur Cluster
(5 more ⇓) 		CSA • PDB • PDBSum
5FES Hyde From T. Maritima In Complex With (2R,4R)-Mesetda [Fefe] Hydrogenase Maturase Subunit Hyde 6 1.27 2-Hydroxy-L-Tyrosine
(5 more ⇓) 		CSA • PDB • PDBSum
5FEP Hyde From T. Maritima In Complex With (2R,4R)-Metda [Fefe] Hydrogenase Maturase Subunit Hyde 6 1.45 2-Hydroxy-L-Tyrosine
(5 more ⇓) 		CSA • PDB • PDBSum
5FEX Hyde From T. Maritima In Complex With Se-Adenosyl-L-Selenocysteine (Tfinal Of The Reaction) [Fefe] Hydrogenase Maturase Subunit Hyde 6 1.32 2-Hydroxy-L-Tyrosine
(6 more ⇓) 		CSA • PDB • PDBSum
5FEW Hyde From T. Maritima In Complex With S-Adenosyl-L-Cysteine (Final Product) [Fefe] Hydrogenase Maturase Subunit Hyde 6 1.17 Iron/Sulfur Cluster
(6 more ⇓) 		CSA • PDB • PDBSum
5FF0 Hyde From T. Maritima In Complex With S-Adenosyl-L-Cysteine And Methionine [Fefe] Hydrogenase Maturase Subunit Hyde 6 1.49 Fe4-Se4 Cluster
(4 more ⇓) 		CSA • PDB • PDBSum
5FEZ Hyde From T. Maritima In Complex With (2R,4R)-Mesetda, 5'-Deoxyadenosine And Methionine [Fefe] Hydrogenase Maturase Subunit Hyde 6 1.35 Fe4-Se4 Cluster
(5 more ⇓) 		CSA • PDB • PDBSum
5FF4 Hyde From T. Maritima In Complex With (2R,4R)-Tmetda [Fefe] Hydrogenase Maturase Subunit Hyde 6 1.35 Fe4-Se4 Cluster
(5 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
May 14, 2014, 3:08 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 332 348
update domain start position 11 1
Sept. 15, 2014, 5:18 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update name [FeFe]-hydrogenase maturase HydE uncharacterized HydE_PylB-like protein
update domain start position 1 4
update subgroup - BATS domain containing
Dec. 17, 2015, 5:52 a.m. update curation agent setDomainBoundaries.py holliday
update name uncharacterized HydE_PylB-like protein uncharacterized HydE/PylB-like sequence
update subgroup BATS domain containing HydE/PylB-like
update superfamily assignment evidence code ISS IEA
Oct. 15, 2016, 6:30 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 348 347
update domain start position 4 5
EC number assigned by UniProtKB accession ID.