Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetylene hydratase

Gene
N/A
Organism
Pelobacter acetylenicus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydration of acetylene to form acetaldehyde. Ethylene cannot act as a substrate.1 Publication

Catalytic activityi

Acetaldehyde = acetylene + H2O.1 Publication

Cofactori

Protein has several cofactor binding sites:

Kineticsi

  1. KM=14 µM for acetylene1 Publication
  1. Vmax=69 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 6.0-6.5.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi9 – 91Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi12 – 121Iron-sulfur (4Fe-4S)1 Publication
Active sitei13 – 131
Metal bindingi16 – 161Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi46 – 461Iron-sulfur (4Fe-4S)1 Publication
Binding sitei48 – 481Molybdopterin guanine dinucleotide 1
Metal bindingi141 – 1411Tungsten
Binding sitei141 – 1411Molybdopterin guanine dinucleotide 1
Binding sitei141 – 1411Molybdopterin guanine dinucleotide 2
Binding sitei296 – 2961Molybdopterin guanine dinucleotide 1
Binding sitei300 – 3001Molybdopterin guanine dinucleotide 1
Binding sitei460 – 4601Molybdopterin guanine dinucleotide 2; via carbonyl oxygen
Binding sitei465 – 4651Molybdopterin guanine dinucleotide 2
Binding sitei606 – 6061Molybdopterin guanine dinucleotide 2
Binding sitei676 – 6761Molybdopterin guanine dinucleotide 2
Binding sitei699 – 6991Molybdopterin guanine dinucleotide 2
Binding sitei720 – 7201Molybdopterin guanine dinucleotide 1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB
  • acetylene hydratase activity Source: UniProtKB
  • molybdenum ion binding Source: InterPro
  • molybdopterin cofactor binding Source: UniProtKB
  • oxidoreductase activity Source: InterPro

GO - Biological processi

  • metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, Tungsten

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-941.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylene hydratase (EC:4.2.1.112)
Short name:
Ahy
OrganismiPelobacter acetylenicus
Taxonomic identifieri29542 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131D → A: Almost abolishes catalytic activity. 1 Publication
Mutagenesisi13 – 131D → E: Does not affect catalytic activity. 1 Publication
Mutagenesisi48 – 481K → A: Does not affect catalytic activity. 1 Publication
Mutagenesisi142 – 1421I → A: Strongly impairs catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 730729Acetylene hydratasePRO_0000418733Add
BLAST

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1
730
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Beta strandi17 – 226Combined sources
Beta strandi28 – 325Combined sources
Beta strandi38 – 403Combined sources
Helixi47 – 504Combined sources
Helixi52 – 565Combined sources
Beta strandi66 – 683Combined sources
Beta strandi70 – 723Combined sources
Beta strandi78 – 803Combined sources
Helixi83 – 10119Combined sources
Helixi103 – 1053Combined sources
Beta strandi106 – 1105Combined sources
Helixi112 – 1143Combined sources
Helixi121 – 1299Combined sources
Helixi137 – 1404Combined sources
Helixi143 – 15311Combined sources
Beta strandi157 – 1593Combined sources
Turni161 – 1633Combined sources
Beta strandi165 – 1717Combined sources
Helixi180 – 19112Combined sources
Beta strandi195 – 1995Combined sources
Helixi205 – 2095Combined sources
Beta strandi211 – 2144Combined sources
Helixi221 – 23414Combined sources
Helixi240 – 2467Combined sources
Helixi250 – 2578Combined sources
Helixi262 – 2698Combined sources
Helixi273 – 28513Combined sources
Beta strandi286 – 2905Combined sources
Helixi296 – 2983Combined sources
Helixi303 – 31715Combined sources
Turni318 – 3214Combined sources
Beta strandi322 – 3276Combined sources
Helixi337 – 3404Combined sources
Helixi343 – 3453Combined sources
Helixi348 – 3536Combined sources
Turni355 – 3595Combined sources
Helixi361 – 3633Combined sources
Helixi365 – 3684Combined sources
Helixi369 – 3713Combined sources
Helixi372 – 3798Combined sources
Helixi394 – 40310Combined sources
Beta strandi411 – 4166Combined sources
Helixi419 – 4213Combined sources
Beta strandi422 – 4243Combined sources
Helixi426 – 4349Combined sources
Beta strandi437 – 4459Combined sources
Helixi450 – 4523Combined sources
Beta strandi454 – 4596Combined sources
Helixi462 – 4643Combined sources
Beta strandi476 – 4794Combined sources
Helixi494 – 50411Combined sources
Helixi508 – 5103Combined sources
Helixi516 – 5238Combined sources
Helixi525 – 5273Combined sources
Helixi531 – 5344Combined sources
Beta strandi537 – 5415Combined sources
Beta strandi556 – 56510Combined sources
Helixi567 – 5726Combined sources
Beta strandi584 – 5863Combined sources
Turni587 – 5893Combined sources
Helixi591 – 5966Combined sources
Beta strandi599 – 6035Combined sources
Helixi620 – 6245Combined sources
Beta strandi629 – 6324Combined sources
Helixi634 – 6407Combined sources
Beta strandi646 – 6516Combined sources
Beta strandi656 – 6638Combined sources
Beta strandi671 – 6744Combined sources
Helixi687 – 6893Combined sources
Turni690 – 6934Combined sources
Helixi694 – 6974Combined sources
Helixi699 – 7024Combined sources
Helixi707 – 7093Combined sources
Turni712 – 7143Combined sources
Beta strandi720 – 72910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E7ZX-ray1.26A4-730[»]
ProteinModelPortaliQ71EW5.
SMRiQ71EW5. Positions 4-730.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ71EW5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 1144MGD 2 binding
Regioni172 – 1732MGD 1 binding
Regioni177 – 1793MGD 1 binding
Regioni199 – 2024MGD 1 binding
Regioni218 – 2214MGD 1 binding
Regioni416 – 4183MGD 2 binding
Regioni422 – 4232MGD 2 binding
Regioni442 – 4443MGD 2 binding
Regioni602 – 61211MGD 1 bindingAdd
BLAST
Regioni612 – 6132MGD 2 binding

Sequence similaritiesi

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
[Graphical view]
PfamiPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q71EW5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKKHVVCQ SCDINCVVEA EVKADGKIQT KSISEPHPTT PPNSICMKSV
60 70 80 90 100
NADTIRTHKD RVLYPLKNVG SKRGEQRWER ISWDQALDEI AEKLKKIIAK
110 120 130 140 150
YGPESLGVSQ TEINQQSEYG TLRRFMNLLG SPNWTSAMYM CIGNTAGVHR
160 170 180 190 200
VTHGSYSFAS FADSNCLLFI GKNLSNHNWV SQFNDLKAAL KRGCKLIVLD
210 220 230 240 250
PRRTKVAEMA DIWLPLRYGT DAALFLGMIN VIINEQLYDK EFVENWCVGF
260 270 280 290 300
EELKERVQEY PLDKVAEITG CDAGEIRKAA VMFATESPAS IPWAVSTDMQ
310 320 330 340 350
KNSCSAIRAQ CILRAIVGSF VNGAEILGAP HSDLVPISKI QMHEALPEEK
360 370 380 390 400
KKLQLGTETY PFLTYTGMSA LEEPSERVYG VKYFHNMGAF MANPTALFTA
410 420 430 440 450
MATEKPYPVK AFFALASNAL MGYANQQNAL KGLMNQDLVV CYDQFMTPTA
460 470 480 490 500
QLADYVLPGD HWLERPVVQP NWEGIPFGNT SQQVVEPAGE AKDEYYFIRE
510 520 530 540 550
LAVRMGLEEH FPWKDRLELI NYRISPTGME WEEYQKQYTY MSKLPDYFGP
560 570 580 590 600
EGVGVATPSG KVELYSSVFE KLGYDPLPYY HEPLQTEISD PELAKEYPLI
610 620 630 640 650
LFAGLREDSN FQSCYHQPGI LRDAEPDPVA LLHPKTAQSL GLPSGEWIWV
660 670 680 690 700
ETTHGRLKLL LKHDGAQPEG TIRIPHGRWC PEQEGGPETG FSGAMLHNDA
710 720 730
MVLSDDDWNL DPEQGLPNLR GGILAKAYKC
Length:730
Mass (Da):81,851
Last modified:July 5, 2004 - v1
Checksum:iBB7E4D5356EE8913
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111S → C AA sequence (PubMed:7592321).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF518725 Genomic DNA. Translation: AAQ08379.1.

Genome annotation databases

KEGGiag:AAQ08379.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF518725 Genomic DNA. Translation: AAQ08379.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E7ZX-ray1.26A4-730[»]
ProteinModelPortaliQ71EW5.
SMRiQ71EW5. Positions 4-730.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAQ08379.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-941.

Miscellaneous databases

EvolutionaryTraceiQ71EW5.

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
[Graphical view]
PfamiPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Evolution of the DMSO-reductase superfamily: A diverse group of Molybdopterin-containing enzymes."
    Abt D.J., Brinkmann H., Meyer A., Schink B., Kroneck P.M.H.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DSM 3246 / NBRC 103808 / WoAcy1.
  2. "Purification and characterization of acetylene hydratase of Pelobacter acetylenicus, a tungsten iron-sulfur protein."
    Rosner B.M., Schink B.
    J. Bacteriol. 177:5767-5772(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
  3. "Acetylene hydratase of Pelobacter acetylenicus. Molecular and spectroscopic properties of the tungsten iron-sulfur enzyme."
    Meckenstock R.U., Krieger R., Ensign S., Kroneck P.M., Schink B.
    Eur. J. Biochem. 264:176-182(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  4. "Exploring the active site of the tungsten, iron-sulfur enzyme acetylene hydratase."
    Tenbrink F., Schink B., Kroneck P.M.
    J. Bacteriol. 193:1229-1236(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-13; LYS-48 AND ILE-142.
  5. "Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase."
    Seiffert G.B., Ullmann G.M., Messerschmidt A., Schink B., Kroneck P.M., Einsle O.
    Proc. Natl. Acad. Sci. U.S.A. 104:3073-3077(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 4-730 IN COMPLEX WITH IRON-SULFUR (4FE-4S) AND W-BIS-MGD, COFACTOR, REACTION MECHANISM.

Entry informationi

Entry nameiAHY_PELAE
AccessioniPrimary (citable) accession number: Q71EW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: July 5, 2004
Last modified: January 20, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The tungsten center binds a water molecule that is activated by Asp-13 residue, enabling it to attack acetylene bound in a distinct hydrophobic pocket.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.