AHY_SYNAC
ID AHY_SYNAC Reviewed; 730 AA.
AC Q71EW5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Acetylene hydratase;
DE Short=Ahy;
DE EC=4.2.1.112 {ECO:0000269|PubMed:7592321};
OS Syntrophotalea acetylenica (Pelobacter acetylenicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=29542;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 3246 / NBRC 103808 / WoAcy1;
RA Abt D.J., Brinkmann H., Meyer A., Schink B., Kroneck P.M.H.;
RT "Evolution of the DMSO-reductase superfamily: A diverse group of
RT Molybdopterin-containing enzymes.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-20, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7592321; DOI=10.1128/jb.177.20.5767-5772.1995;
RA Rosner B.M., Schink B.;
RT "Purification and characterization of acetylene hydratase of Pelobacter
RT acetylenicus, a tungsten iron-sulfur protein.";
RL J. Bacteriol. 177:5767-5772(1995).
RN [3]
RP COFACTOR.
RX PubMed=10447686; DOI=10.1046/j.1432-1327.1999.00600.x;
RA Meckenstock R.U., Krieger R., Ensign S., Kroneck P.M., Schink B.;
RT "Acetylene hydratase of Pelobacter acetylenicus. Molecular and
RT spectroscopic properties of the tungsten iron-sulfur enzyme.";
RL Eur. J. Biochem. 264:176-182(1999).
RN [4]
RP MUTAGENESIS OF ASP-13; LYS-48 AND ILE-142.
RX PubMed=21193613; DOI=10.1128/jb.01057-10;
RA Tenbrink F., Schink B., Kroneck P.M.;
RT "Exploring the active site of the tungsten, iron-sulfur enzyme acetylene
RT hydratase.";
RL J. Bacteriol. 193:1229-1236(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 4-730 IN COMPLEX WITH IRON-SULFUR
RP (4FE-4S) AND W-BIS-MGD, COFACTOR, AND REACTION MECHANISM.
RX PubMed=17360611; DOI=10.1073/pnas.0610407104;
RA Seiffert G.B., Ullmann G.M., Messerschmidt A., Schink B., Kroneck P.M.,
RA Einsle O.;
RT "Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene
RT hydratase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3073-3077(2007).
CC -!- FUNCTION: Catalyzes the hydration of acetylene to form acetaldehyde.
CC Ethylene cannot act as a substrate. {ECO:0000269|PubMed:7592321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde = acetylene + H2O; Xref=Rhea:RHEA:17885,
CC ChEBI:CHEBI:15343, ChEBI:CHEBI:15377, ChEBI:CHEBI:27518;
CC EC=4.2.1.112; Evidence={ECO:0000269|PubMed:7592321};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:17360611};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:17360611};
CC -!- COFACTOR:
CC Name=W-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60537;
CC Evidence={ECO:0000269|PubMed:17360611};
CC Note=Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD)
CC cofactor per subunit. {ECO:0000269|PubMed:17360611};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for acetylene {ECO:0000269|PubMed:7592321};
CC Vmax=69 umol/min/mg enzyme {ECO:0000269|PubMed:7592321};
CC pH dependence:
CC Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:7592321};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:7592321};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17360611,
CC ECO:0000269|PubMed:7592321}.
CC -!- MISCELLANEOUS: The tungsten center binds a water molecule that is
CC activated by Asp-13 residue, enabling it to attack acetylene bound in a
CC distinct hydrophobic pocket. {ECO:0000305|PubMed:17360611}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AF518725; AAQ08379.1; -; Genomic_DNA.
DR PDB; 2E7Z; X-ray; 1.26 A; A=4-730.
DR PDBsum; 2E7Z; -.
DR AlphaFoldDB; Q71EW5; -.
DR SMR; Q71EW5; -.
DR STRING; 29542.A6070_04635; -.
DR KEGG; ag:AAQ08379; -.
DR BioCyc; MetaCyc:MON-941; -.
DR BRENDA; 4.2.1.112; 8840.
DR EvolutionaryTrace; Q71EW5; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0018818; F:acetylene hydratase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02759; MopB_Acetylene-hydratase; 1.
DR CDD; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR InterPro; IPR041930; Acetylene_hydratase.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Lyase;
KW Metal-binding; Tungsten.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7592321"
FT CHAIN 2..730
FT /note="Acetylene hydratase"
FT /id="PRO_0000418733"
FT ACT_SITE 13
FT BINDING 9
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 48
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 111..114
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 141
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /ligand_part="W"
FT /ligand_part_id="ChEBI:CHEBI:27998"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 172..173
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 177..179
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 199..202
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 218..221
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 296
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 300
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 416..418
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 422..423
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 442..444
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 460
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 465
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 602..613
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 606
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 676
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 699
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT BINDING 720
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /evidence="ECO:0000269|PubMed:17360611"
FT MUTAGEN 13
FT /note="D->A: Almost abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21193613"
FT MUTAGEN 13
FT /note="D->E: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:21193613"
FT MUTAGEN 48
FT /note="K->A: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:21193613"
FT MUTAGEN 142
FT /note="I->A: Strongly impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:21193613"
FT CONFLICT 11
FT /note="S -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 83..101
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2E7Z"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 273..285
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 303..317
FT /evidence="ECO:0007829|PDB:2E7Z"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 348..353
FT /evidence="ECO:0007829|PDB:2E7Z"
FT TURN 355..359
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 372..379
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 394..403
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 426..434
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 437..445
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 494..504
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 516..523
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 531..534
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 556..565
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 567..572
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:2E7Z"
FT TURN 587..589
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 591..596
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 599..603
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 620..624
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 634..640
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 646..651
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 656..663
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 687..689
FT /evidence="ECO:0007829|PDB:2E7Z"
FT TURN 690..693
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 694..697
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 699..702
FT /evidence="ECO:0007829|PDB:2E7Z"
FT HELIX 707..709
FT /evidence="ECO:0007829|PDB:2E7Z"
FT TURN 712..714
FT /evidence="ECO:0007829|PDB:2E7Z"
FT STRAND 720..729
FT /evidence="ECO:0007829|PDB:2E7Z"
SQ SEQUENCE 730 AA; 81851 MW; BB7E4D5356EE8913 CRC64;
MASKKHVVCQ SCDINCVVEA EVKADGKIQT KSISEPHPTT PPNSICMKSV NADTIRTHKD
RVLYPLKNVG SKRGEQRWER ISWDQALDEI AEKLKKIIAK YGPESLGVSQ TEINQQSEYG
TLRRFMNLLG SPNWTSAMYM CIGNTAGVHR VTHGSYSFAS FADSNCLLFI GKNLSNHNWV
SQFNDLKAAL KRGCKLIVLD PRRTKVAEMA DIWLPLRYGT DAALFLGMIN VIINEQLYDK
EFVENWCVGF EELKERVQEY PLDKVAEITG CDAGEIRKAA VMFATESPAS IPWAVSTDMQ
KNSCSAIRAQ CILRAIVGSF VNGAEILGAP HSDLVPISKI QMHEALPEEK KKLQLGTETY
PFLTYTGMSA LEEPSERVYG VKYFHNMGAF MANPTALFTA MATEKPYPVK AFFALASNAL
MGYANQQNAL KGLMNQDLVV CYDQFMTPTA QLADYVLPGD HWLERPVVQP NWEGIPFGNT
SQQVVEPAGE AKDEYYFIRE LAVRMGLEEH FPWKDRLELI NYRISPTGME WEEYQKQYTY
MSKLPDYFGP EGVGVATPSG KVELYSSVFE KLGYDPLPYY HEPLQTEISD PELAKEYPLI
LFAGLREDSN FQSCYHQPGI LRDAEPDPVA LLHPKTAQSL GLPSGEWIWV ETTHGRLKLL
LKHDGAQPEG TIRIPHGRWC PEQEGGPETG FSGAMLHNDA MVLSDDDWNL DPEQGLPNLR
GGILAKAYKC
