CCR_STRAW
ID CCR_STRAW Reviewed; 445 AA.
AC Q82LU9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Crotonyl-CoA reductase;
DE EC=1.3.1.86;
GN Name=ccrA2; OrderedLocusNames=SAV_1911;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION AS A CROTONYL-COA REDUCTASE,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=8521864; DOI=10.1111/j.1432-1033.1995.954_3.x;
RA Wallace K.K., Bao Z.Y., Dai H., Digate R., Schuler G., Speedie M.K.,
RA Reynolds K.A.;
RT "Purification of crotonyl-CoA reductase from Streptomyces collinus and
RT cloning, sequencing and expression of the corresponding gene in Escherichia
RT coli.";
RL Eur. J. Biochem. 233:954-962(1995).
CC -!- FUNCTION: Catalyzes the conversion of crotonyl-CoA to butyryl-CoA. It
CC uses only NADP as electron donor. May have a role in providing butyryl-
CC CoA as a starter unit for straight-chain fatty acid biosynthesis.
CC {ECO:0000269|PubMed:8521864}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + NADP(+) = (2E)-butenoyl-CoA + H(+) + NADPH;
CC Xref=Rhea:RHEA:27906, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.86;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by NADPH at concentrations above 200 uM,
CC by MgCl (30%), by ZnCl(2) (55%), and by CoCl, MnCl and CaCl (100%).
CC Also inhibited by iodoacetamide, N-ethylmaleamide, the thiol group
CC inhibitor beta-chloromercuribenzoate, palmitoyl-CoA and myristoyl-CoA.
CC {ECO:0000269|PubMed:8521864}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for NADP (at 30 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:8521864};
CC KM=18 uM for crotonyl-CoA (at 30 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:8521864};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:8521864};
CC Temperature dependence:
CC Optimum temperature 40 degrees Celsius. {ECO:0000269|PubMed:8521864};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8521864}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Crotonyl-CoA carboxylase/reductase subfamily. {ECO:0000305}.
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; BA000030; BAC69622.1; -; Genomic_DNA.
DR RefSeq; WP_010983350.1; NZ_JZJK01000086.1.
DR AlphaFoldDB; Q82LU9; -.
DR SMR; Q82LU9; -.
DR STRING; 227882.SAV_1911; -.
DR PRIDE; Q82LU9; -.
DR EnsemblBacteria; BAC69622; BAC69622; SAVERM_1911.
DR KEGG; sma:SAVERM_1911; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_5_0_11; -.
DR OMA; DFNCWGQ; -.
DR OrthoDB; 884088at2; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0043880; F:crotonyl-CoA reductase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
DR CDD; cd08246; crotonyl_coA_red; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR010085; Crot_CoA_red.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
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 TIGRFAMs; TIGR01751; crot-CoA-red; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..445
FT /note="Crotonyl-CoA reductase"
FT /id="PRO_0000418981"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 445 AA; 49160 MW; 483273D9A2FA647C CRC64;
MKEILDAIQS QTATSADFAA LPLPDSYRAI TVHKDETEMF AGLSTRDKDP RKSIHLDDVP
VPELGPGEAL VAVMASSVNY NSVWTSIFEP VSTFNFLERY GRLSDLSKRH DLPYHIIGSD
LAGVVLRTGP GVNSWKPGDE VVAHCLSVEL ESSDGHNDTM LDPEQRIWGF ETNFGGLAEI
ALVKSNQLMP KPDHLSWEEA AAPGLVNSTA YRQLVSRNGA GMKQGDNVLI WGASGGLGSY
ATQFALAGGA NPICVVSSEQ KADICRSMGA EAIIDRNAEG YKFWKDETTQ DPKEWKRFGK
RIREFTGGED IDIVFEHPGR ETFGASVYVT RKGGTITTCA STSGYMHEYD NRYLWMSLKR
IIGSHFANYR EAWEANRLVA KGKIHPTLSK VYSLEDTGQA AYDVHRNLHQ GKVGVLALAP
REGLGVRDEE KRAQHIDAIN RFRNI
