ACAR_SULTO
ID ACAR_SULTO Reviewed; 334 AA.
AC Q975C8; B8XVT1;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=STK_04800;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1] {ECO:0000312|EMBL:BAB65473.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
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. Inactive
CC towards 3-hydroxypropionyl-CoA, NADH and crotonyl-CoA.
CC {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:0000269|PubMed:19429610};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for NADPH {ECO:0000269|PubMed:19429610};
CC KM=3 uM for acryloyl-CoA {ECO:0000269|PubMed:19429610};
CC pH dependence:
CC Optimum pH is 6.0 at 65 degrees Celsius. Retains half maximum
CC activity at pH 7.5 at 65 degrees Celsius.
CC {ECO:0000269|PubMed:19429610};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19429610}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000255}.
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DR EMBL; BA000023; BAB65473.1; -; Genomic_DNA.
DR EMBL; FJ445417; ACJ71675.1; -; Genomic_DNA.
DR RefSeq; WP_010978456.1; NC_003106.2.
DR AlphaFoldDB; Q975C8; -.
DR SMR; Q975C8; -.
DR STRING; 273063.STK_04800; -.
DR EnsemblBacteria; BAB65473; BAB65473; STK_04800.
DR GeneID; 1458422; -.
DR KEGG; sto:STK_04800; -.
DR PATRIC; fig|273063.9.peg.554; -.
DR eggNOG; arCOG01455; Archaea.
DR OMA; VWSNVFM; -.
DR OrthoDB; 56644at2157; -.
DR BioCyc; MetaCyc:MON-13730; -.
DR BRENDA; 1.3.1.84; 15396.
DR SABIO-RK; Q975C8; -.
DR Proteomes; UP000001015; 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..334
FT /note="Acryloyl-coenzyme A reductase"
FT /id="PRO_0000404602"
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 173..176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 195..197
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 334 AA; 36300 MW; 6CA4998B7EAE4D95 CRC64;
MKAIVVPGPK QGYKLEEVPD PKPGKDEVII RVDRAALCYR DLLQLQGYYP RMKYPVILGH
EVVGTIEEVG ENIKGFEVGD KVISLLYAPD GTCEYCQIGE EAYCHHRLGY SEELDGFFAE
KAKIKVTSLV KVPKGTPDEG AVLVPCVTGM IYRGIRRAGG IRKGELVLVT GASGGVGIHA
IQVAKALGAK VIGVTTSEEK AKIIKQYADY VIVGTKFSEE AKKIGDVTLV IDTVGTPTFD
ESLKSLWMGG RIVQIGNVDP SQIYNLRLGY IILKDLKIVG HASATKKDAE DTLKLTQEGK
IKPVIAGTVS LENIDEGYKM IKDKNKVGKV LVKP
