ACAR_METS5
ID ACAR_METS5 Reviewed; 332 AA.
AC A4YGN2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Acryloyl-coenzyme A reductase {ECO:0000303|PubMed:19429610};
DE Short=Acryloyl-CoA reductase {ECO:0000303|PubMed:19429610};
DE EC=1.3.1.84;
GN OrderedLocusNames=Msed_1426;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABP95584.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
RN [2] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=19429610; DOI=10.1128/jb.00068-09;
RA Teufel R., Kung J.W., Kockelkorn D., Alber B.E., Fuchs G.;
RT "3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A
RT reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate
RT cycle in the Sulfolobales.";
RL J. Bacteriol. 191:4572-4581(2009).
CC -!- FUNCTION: Plays a role in autotrophic carbon fixation via the 3-
CC hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the acryloyl-CoA
CC dependent NADPH oxidation and formation of propionyl-CoA.
CC {ECO:0000250|UniProtKB:Q975C8, ECO:0000269|PubMed:19429610}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADPH;
CC Xref=Rhea:RHEA:26454, ChEBI:CHEBI:15378, ChEBI:CHEBI:57367,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.84;
CC Evidence={ECO:0000269|PubMed:19429610};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q975C8};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q975C8}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000682; ABP95584.1; -; Genomic_DNA.
DR RefSeq; WP_012021371.1; NC_009440.1.
DR AlphaFoldDB; A4YGN2; -.
DR SMR; A4YGN2; -.
DR STRING; 399549.Msed_1426; -.
DR EnsemblBacteria; ABP95584; ABP95584; Msed_1426.
DR GeneID; 5104797; -.
DR GeneID; 59457466; -.
DR KEGG; mse:Msed_1426; -.
DR eggNOG; arCOG01455; Archaea.
DR HOGENOM; CLU_026673_11_0_2; -.
DR OMA; FWGEFAR; -.
DR BRENDA; 1.3.1.84; 7245.
DR Proteomes; UP000000242; Chromosome.
DR GO; GO:0043957; F:acryloyl-CoA reductase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043958; F:acryloyl-CoA reductase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..332
FT /note="Acryloyl-coenzyme A reductase"
FT /id="PRO_0000404648"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P39462"
FT BINDING 39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P39462"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39462"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39462"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39462"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39462"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P39462"
FT BINDING 172..175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 194..196
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 332 AA; 36037 MW; CEC1CA5A3B73E6A4 CRC64;
MKAVVVKGHK QGYEVREVQD PKPASGEVII KVRRAALCYR DLLQLQGFYP RMKYPVVLGH
EVVGEILEVG EGVTGFSPGD RVISLLYAPD GTCHYCRQGE EAYCHSRLGY SEELDGFFSE
MAKVKVTSLV KVPTRASDEG AVMVPCVTGM VYRGLRRANL REGETVLVTG ASGGVGIHAL
QVAKAMGARV VGVTTSEEKA SIVGKYADRV IVGSKFSEEA KKEDINVVID TVGTPTFDES
LKSLWMGGRI VQIGNVDPTQ SYQLRLGYTI LKDIAIIGHA SATRRDAEGA LKLTAEGKIR
PVVAGTVHLE EIDKGYEMLK DKHKVGKVLL TT
