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Protein

[FeFe] hydrogenase maturase subunit HydE

Gene

TM_1269

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for the maturation of the [FeFe]-hydrogenase HydA (By similarity). Catalyzes the reductive cleavage of S-adenosyl-L-methionine (in vitro), suggesting it may contribute to the biosynthesis of an essential sulfur-containing ligand that binds to the hydrogenase active site [2Fe-2S] cluster (PubMed:16137685).By similarityCurated1 Publication

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotationCombined sources3 Publications
Metal bindingi67 – 671Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotationCombined sources1 Publication
Metal bindingi70 – 701Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotationCombined sources1 Publication
Metal bindingi311 – 3111Iron-sulfur (2Fe-2S)Combined sources
Metal bindingi319 – 3191Iron-sulfur (2Fe-2S)Combined sources
Metal bindingi322 – 3221Iron-sulfur (2Fe-2S)Combined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciTMAR243274:GC6P-1300-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
[FeFe] hydrogenase maturase subunit HydECurated (EC:1.8.-.-Curated)
Gene namesi
Ordered Locus Names:TM_1269Imported
ORF Names:THEMA_07990Imported, Tmari_1274Imported
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)Imported
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000013901 Componenti: Chromosome
  • UP000008183 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631C → A: Eliminates binding of one iron-sulfur cluster; when associated with A-67 and A-70. 1 Publication
Mutagenesisi67 – 671C → A: Eliminates binding of one iron-sulfur cluster; when associated with A-63 and A-70. 1 Publication
Mutagenesisi70 – 701C → A: Eliminates binding of one iron-sulfur cluster; when associated with A-63 and A-67. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348[FeFe] hydrogenase maturase subunit HydEPRO_0000433230Add
BLAST

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi243274.TM1269.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Helixi17 – 259Combined sources
Helixi29 – 4719Combined sources
Beta strandi49 – 6012Combined sources
Helixi86 – 9813Combined sources
Beta strandi102 – 1098Combined sources
Helixi112 – 1143Combined sources
Helixi117 – 12711Combined sources
Turni128 – 1303Combined sources
Beta strandi132 – 1365Combined sources
Helixi142 – 15110Combined sources
Beta strandi155 – 1573Combined sources
Helixi165 – 1717Combined sources
Helixi177 – 18913Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi198 – 2014Combined sources
Helixi207 – 22014Combined sources
Beta strandi223 – 2253Combined sources
Turni237 – 2404Combined sources
Helixi246 – 25914Combined sources
Helixi269 – 2746Combined sources
Helixi278 – 2836Combined sources
Turni284 – 2863Combined sources
Turni297 – 2993Combined sources
Helixi300 – 3023Combined sources
Beta strandi305 – 3073Combined sources
Turni310 – 3134Combined sources
Helixi319 – 32911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CIWX-ray1.35A1-348[»]
3CIXX-ray1.70A1-348[»]
3IIXX-ray1.25A1-348[»]
3IIZX-ray1.62A1-348[»]
4JXCX-ray1.50A1-348[»]
4JY8X-ray2.90A2-348[»]
4JY9X-ray1.60A1-348[»]
4JYDX-ray1.71A1-348[»]
4JYEX-ray1.65A1-348[»]
4JYFX-ray1.45A1-348[»]
ProteinModelPortaliQ9X0Z6.
SMRiQ9X0Z6. Positions 2-347.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. HydE family.Curated

Phylogenomic databases

eggNOGiENOG4107QW8. Bacteria.
COG0502. LUCA.
KOiK01012.
OMAiFLLRHET.
OrthoDBiEOG6FJNBQ.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR006638. Elp3/MiaB/NifB.
IPR024021. FeFe-hyd_HydE_rSAM.
IPR005244. FO_synthase_su2-like.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF004762. CHP00423. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03956. rSAM_HydE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9X0Z6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGREILEKL ERREFTREVL KEALSINDRG FNEALFKLAD EIRRKYVGDE
60 70 80 90 100
VHIRAIIEFS NVCRKNCLYC GLRRDNKNLK RYRMTPEEIV ERARLAVQFG
110 120 130 140 150
AKTIVLQSGE DPYYMPDVIS DIVKEIKKMG VAVTLSLGEW PREYYEKWKE
160 170 180 190 200
AGADRYLLRH ETANPVLHRK LRPDTSFENR LNCLLTLKEL GYETGAGSMV
210 220 230 240 250
GLPGQTIDDL VDDLLFLKEH DFDMVGIGPF IPHPDTPLAN EKKGDFTLTL
260 270 280 290 300
KMVALTRILL PDSNIPATTA MGTIVPGGRE ITLRCGANVI MPNWTPSPYR
310 320 330 340
QLYQLYPGKI CVFEKDTACI PCVMKMIELL GRKPGRDWGG RKRVFETV
Length:348
Mass (Da):39,799
Last modified:November 1, 1999 - v1
Checksum:i472505213FF63799
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36344.1.
CP004077 Genomic DNA. Translation: AGL50198.1.
CP007013 Genomic DNA. Translation: AHD18826.1.
PIRiD72274.
RefSeqiNP_229074.1. NC_000853.1.
WP_004079975.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36344; AAD36344; TM_1269.
AGL50198; AGL50198; Tmari_1274.
AHD18826; AHD18826; THEMA_07990.
GeneIDi898214.
KEGGitma:TM1269.
tmi:THEMA_07990.
tmm:Tmari_1274.
tmw:THMA_1294.
PATRICi23937478. VBITheMar51294_1285.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36344.1.
CP004077 Genomic DNA. Translation: AGL50198.1.
CP007013 Genomic DNA. Translation: AHD18826.1.
PIRiD72274.
RefSeqiNP_229074.1. NC_000853.1.
WP_004079975.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CIWX-ray1.35A1-348[»]
3CIXX-ray1.70A1-348[»]
3IIXX-ray1.25A1-348[»]
3IIZX-ray1.62A1-348[»]
4JXCX-ray1.50A1-348[»]
4JY8X-ray2.90A2-348[»]
4JY9X-ray1.60A1-348[»]
4JYDX-ray1.71A1-348[»]
4JYEX-ray1.65A1-348[»]
4JYFX-ray1.45A1-348[»]
ProteinModelPortaliQ9X0Z6.
SMRiQ9X0Z6. Positions 2-347.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1269.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36344; AAD36344; TM_1269.
AGL50198; AGL50198; Tmari_1274.
AHD18826; AHD18826; THEMA_07990.
GeneIDi898214.
KEGGitma:TM1269.
tmi:THEMA_07990.
tmm:Tmari_1274.
tmw:THMA_1294.
PATRICi23937478. VBITheMar51294_1285.

Phylogenomic databases

eggNOGiENOG4107QW8. Bacteria.
COG0502. LUCA.
KOiK01012.
OMAiFLLRHET.
OrthoDBiEOG6FJNBQ.

Enzyme and pathway databases

BioCyciTMAR243274:GC6P-1300-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR006638. Elp3/MiaB/NifB.
IPR024021. FeFe-hyd_HydE_rSAM.
IPR005244. FO_synthase_su2-like.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF004762. CHP00423. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03956. rSAM_HydE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  3. "Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima."
    Rubach J.K., Brazzolotto X., Gaillard J., Fontecave M.
    FEBS Lett. 579:5055-5060(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, COFACTOR, MUTAGENESIS OF CYS-63; CYS-67 AND CYS-70.
  4. "X-ray structure of the [FeFe]-hydrogenase maturase HydE from Thermotoga maritima."
    Nicolet Y., Rubach J.K., Posewitz M.C., Amara P., Mathevon C., Atta M., Fontecave M., Fontecilla-Camps J.C.
    J. Biol. Chem. 283:18861-18872(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S); IRON-SULFUR (4FE-4S-S-ADOMET), SUBUNIT, COFACTOR.
  5. "Unexpected electron transfer mechanism upon AdoMet cleavage in radical SAM proteins."
    Nicolet Y., Amara P., Mouesca J.M., Fontecilla-Camps J.C.
    Proc. Natl. Acad. Sci. U.S.A. 106:14867-14871(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S) AND IRON-SULFUR (4FE-4S-S-ADOMET), COFACTOR.
  6. "X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters."
    Nicolet Y., Rohac R., Martin L., Fontecilla-Camps J.C.
    Proc. Natl. Acad. Sci. U.S.A. 110:7188-7192(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S) AND IRON-SULFUR (4FE-4S-S-ADOMET), COFACTOR.

Entry informationi

Entry nameiHYDE_THEMA
AccessioniPrimary (citable) accession number: Q9X0Z6
Secondary accession number(s): G4FE79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 24, 2015
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.