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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)DescriptionActionsGraphical viewLength
Metal bindingi9Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi12Iron-sulfur (4Fe-4S)1 Publication1
Active sitei131
Metal bindingi16Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi46Iron-sulfur (4Fe-4S)1 Publication1
Binding sitei48Molybdopterin guanine dinucleotide 11
Metal bindingi141Tungsten1
Binding sitei141Molybdopterin guanine dinucleotide 11
Binding sitei141Molybdopterin guanine dinucleotide 21
Binding sitei296Molybdopterin guanine dinucleotide 11
Binding sitei300Molybdopterin guanine dinucleotide 11
Binding sitei460Molybdopterin guanine dinucleotide 2; via carbonyl oxygen1
Binding sitei465Molybdopterin guanine dinucleotide 21
Binding sitei606Molybdopterin guanine dinucleotide 21
Binding sitei676Molybdopterin guanine dinucleotide 21
Binding sitei699Molybdopterin guanine dinucleotide 21
Binding sitei720Molybdopterin guanine dinucleotide 11

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 lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesDesulfuromonadaceaePelobacter

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi13D → A: Almost abolishes catalytic activity. 1 Publication1
Mutagenesisi13D → E: Does not affect catalytic activity. 1 Publication1
Mutagenesisi48K → A: Does not affect catalytic activity. 1 Publication1
Mutagenesisi142I → A: Strongly impairs catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00004187332 – 730Acetylene hydrataseAdd BLAST729

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1730
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Beta strandi17 – 22Combined sources6
Beta strandi28 – 32Combined sources5
Beta strandi38 – 40Combined sources3
Helixi47 – 50Combined sources4
Helixi52 – 56Combined sources5
Beta strandi66 – 68Combined sources3
Beta strandi70 – 72Combined sources3
Beta strandi78 – 80Combined sources3
Helixi83 – 101Combined sources19
Helixi103 – 105Combined sources3
Beta strandi106 – 110Combined sources5
Helixi112 – 114Combined sources3
Helixi121 – 129Combined sources9
Helixi137 – 140Combined sources4
Helixi143 – 153Combined sources11
Beta strandi157 – 159Combined sources3
Turni161 – 163Combined sources3
Beta strandi165 – 171Combined sources7
Helixi180 – 191Combined sources12
Beta strandi195 – 199Combined sources5
Helixi205 – 209Combined sources5
Beta strandi211 – 214Combined sources4
Helixi221 – 234Combined sources14
Helixi240 – 246Combined sources7
Helixi250 – 257Combined sources8
Helixi262 – 269Combined sources8
Helixi273 – 285Combined sources13
Beta strandi286 – 290Combined sources5
Helixi296 – 298Combined sources3
Helixi303 – 317Combined sources15
Turni318 – 321Combined sources4
Beta strandi322 – 327Combined sources6
Helixi337 – 340Combined sources4
Helixi343 – 345Combined sources3
Helixi348 – 353Combined sources6
Turni355 – 359Combined sources5
Helixi361 – 363Combined sources3
Helixi365 – 368Combined sources4
Helixi369 – 371Combined sources3
Helixi372 – 379Combined sources8
Helixi394 – 403Combined sources10
Beta strandi411 – 416Combined sources6
Helixi419 – 421Combined sources3
Beta strandi422 – 424Combined sources3
Helixi426 – 434Combined sources9
Beta strandi437 – 445Combined sources9
Helixi450 – 452Combined sources3
Beta strandi454 – 459Combined sources6
Helixi462 – 464Combined sources3
Beta strandi476 – 479Combined sources4
Helixi494 – 504Combined sources11
Helixi508 – 510Combined sources3
Helixi516 – 523Combined sources8
Helixi525 – 527Combined sources3
Helixi531 – 534Combined sources4
Beta strandi537 – 541Combined sources5
Beta strandi556 – 565Combined sources10
Helixi567 – 572Combined sources6
Beta strandi584 – 586Combined sources3
Turni587 – 589Combined sources3
Helixi591 – 596Combined sources6
Beta strandi599 – 603Combined sources5
Helixi620 – 624Combined sources5
Beta strandi629 – 632Combined sources4
Helixi634 – 640Combined sources7
Beta strandi646 – 651Combined sources6
Beta strandi656 – 663Combined sources8
Beta strandi671 – 674Combined sources4
Helixi687 – 689Combined sources3
Turni690 – 693Combined sources4
Helixi694 – 697Combined sources4
Helixi699 – 702Combined sources4
Helixi707 – 709Combined sources3
Turni712 – 714Combined sources3
Beta strandi720 – 729Combined sources10

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ71EW5.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni111 – 114MGD 2 binding4
Regioni172 – 173MGD 1 binding2
Regioni177 – 179MGD 1 binding3
Regioni199 – 202MGD 1 binding4
Regioni218 – 221MGD 1 binding4
Regioni416 – 418MGD 2 binding3
Regioni422 – 423MGD 2 binding2
Regioni442 – 444MGD 2 binding3
Regioni602 – 612MGD 1 bindingAdd BLAST11
Regioni612 – 613MGD 2 binding2

Sequence similaritiesi

Phylogenomic databases

KOiK20625.

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)DescriptionActionsGraphical viewLength
Sequence conflicti11S → C AA sequence (PubMed:7592321).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E7ZX-ray1.26A4-730[»]
ProteinModelPortaliQ71EW5.
SMRiQ71EW5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAQ08379.

Phylogenomic databases

KOiK20625.

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...

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: November 2, 2016
This is version 60 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.