ACRC_ANAPI
ID ACRC_ANAPI Reviewed; 394 AA.
AC G3KIM8;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Acryloyl-CoA reductase (NADH);
DE EC=1.3.1.95;
DE AltName: Full=Propionyl-CoA dehydrogenase;
GN Name=acrC;
OS Anaerotignum propionicum (Clostridium propionicum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerotignum.
OX NCBI_TaxID=28446;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2;
RA Poehlein A., Schlien K., Daniel R., Gottschalk G., Buckel W.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2;
RX PubMed=22810300; DOI=10.1007/s00253-012-4274-y;
RA Kandasamy V., Vaidyanathan H., Djurdjevic I., Jayamani E.,
RA Ramachandran K.B., Buckel W., Jayaraman G., Ramalingam S.;
RT "Engineering Escherichia coli with acrylate pathway genes for propionic
RT acid synthesis and its impact on mixed-acid fermentation.";
RL Appl. Microbiol. Biotechnol. 97:1191-1200(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, MASS SPECTROMETRY, SUBSTRATE SPECIFICITY, AND
RP SUBUNIT.
RC STRAIN=ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2;
RX PubMed=12603323; DOI=10.1046/j.1432-1033.2003.03450.x;
RA Hetzel M., Brock M., Selmer T., Pierik A.J., Golding B.T., Buckel W.;
RT "Acryloyl-CoA reductase from Clostridium propionicum. An enzyme complex of
RT propionyl-CoA dehydrogenase and electron-transferring flavoprotein.";
RL Eur. J. Biochem. 270:902-910(2003).
CC -!- FUNCTION: Probable catalytic subunit of the acryloyl-CoA reductase
CC complex involved in the pathway of L-alanine fermentation. Catalyzes
CC the irreversible NADH-dependent formation of propionyl-CoA from
CC acryloyl-CoA. It can also use 3-buten-2-one as substrate.
CC {ECO:0000269|PubMed:12603323}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:34471, ChEBI:CHEBI:15378, ChEBI:CHEBI:57367,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.95;
CC Evidence={ECO:0000269|PubMed:12603323};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12603323};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 uM for acryloyl-CoA (with NADH as electron acceptor at pH 7.5
CC and 25 degrees Celsius) {ECO:0000269|PubMed:12603323};
CC KM=8 uM for NADH (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12603323};
CC KM=50 uM for propionyl-CoA (with of ferricenium hexafluorophosphate
CC as electron acceptor at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12603323};
CC KM=100 uM for butyryl-CoA (with of ferricenium hexafluorophosphate as
CC electron acceptor at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12603323};
CC KM=1800 uM for 3-buten-2-one (with NADH as electron acceptor at pH
CC 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323};
CC Vmax=0.8 umol/min/mg enzyme with propionyl-CoA as substrate (with
CC ferricenium hexafluorophosphate as electron acceptor at pH 7.5 and 25
CC degrees Celsius) {ECO:0000269|PubMed:12603323};
CC Vmax=1.4 umol/min/mg enzyme with butyryl-CoA as substrate (with
CC ferricenium hexafluorophosphate as electron acceptor at pH 7.5 and 25
CC degrees Celsius) {ECO:0000269|PubMed:12603323};
CC Vmax=1.4 umol/min/mg enzyme with NADH as substrate (at pH 7.5 and 25
CC degrees Celsius) {ECO:0000269|PubMed:12603323};
CC Vmax=1.8 umol/min/mg enzyme with acryloyl-CoA as substrate (with NADH
CC as electron acceptor at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12603323};
CC Vmax=11.6 umol/min/mg enzyme with 3-buten-2-one as substrate (with
CC NADH as electron acceptor at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12603323};
CC Note=kcat is 4.5 sec(-1), 29 sec(-1), 2 sec(-1) and 3.5 sec(-1) for
CC acryloyl-CoA, 3-buten-2-one, propionyl-CoA and butyryl-CoA,
CC respectively (at pH 7.5 and 25 degrees Celsius).;
CC pH dependence:
CC Optimum pH is between 6.5 and 7. {ECO:0000269|PubMed:12603323};
CC Temperature dependence:
CC In the range between 25 and 55 degrees Celsius, the activity
CC increases with rising temperature. Above 55 degrees Celsius, it
CC decreases and becomes almost zero at 65 degrees Celsius.
CC {ECO:0000269|PubMed:12603323};
CC -!- SUBUNIT: Heterohexadecamer; tetramer of tetramers. Each tetramer is
CC composed of 2 alpha (AcrC), a beta (AcrA) and a gamma (AcrB) subunit.
CC {ECO:0000269|PubMed:12603323}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12603323}.
CC -!- MASS SPECTROMETRY: Mass=41440; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12603323};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; JN244656; AEM62998.1; -; Genomic_DNA.
DR AlphaFoldDB; G3KIM8; -.
DR SMR; G3KIM8; -.
DR KEGG; ag:AEM62998; -.
DR BioCyc; MetaCyc:MON-12757; -.
DR SABIO-RK; G3KIM8; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043958; F:acryloyl-CoA reductase activity; IEA:RHEA.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase.
FT CHAIN 1..394
FT /note="Acryloyl-CoA reductase (NADH)"
FT /id="PRO_0000424270"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 135..144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170..172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 254..257
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 350..354
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 379..381
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 394 AA; 42781 MW; 6FB4A2DB12D901C2 CRC64;
MFLLKIKKER MKRMDFSLTR EQEMLKKLAR QFAEIELEPV AEEIDREHVF PAENFKKMAE
IGLTGIGIPK EFGGSGGGTL EKVIAVSEFG KKCMASASIL SIHLIAPQAI YKYGTKEQKE
TYLPRLTKGG ELGAFALTEP NAGSDAGAVK TTAILDSQTN EYVLNGTKCF ISGGGRAGVL
VIFALTEPKK GLKGMSAIIV EKGTPGFSIG KVESKMGIAG SETAELIFED CRVPAANLLG
KEGKGFKIAM EALDGARIGV GAQAIGIAEG AIDLSVKYVH ERIQFGKPIA NLQGIQWYIA
DMATKTAAAR ALVEFAAYLE DAGKPFTKES AMCKLNASEN ARFVTNLALQ IHGGYGYMKD
YPLERMYRDA KITEIYEGTS EIHKVVIARE VMKR
