CCR_STRCU
ID CCR_STRCU Reviewed; 447 AA.
AC Q53865;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Crotonyl-CoA reductase;
DE EC=1.3.1.86;
GN Name=ccr;
OS Streptomyces collinus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=42684;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A CROTONYL-COA REDUCTASE,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=Tu 1892;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), AND SUBUNIT.
RA Scarsdale J.N., Musayev F.N., Hazzard C., Florova G., Reynolds K.,
RA Wright H.T.;
RT "Structure of Streptomycs collinus crotonyl COA carboxylase/reductase.";
RL Submitted (JUN-2009) to the PDB data bank.
CC -!- FUNCTION: May play a role in supplying butyryl-CoA for straight-chain
CC fatty acid biosynthesis. Catalyzes the conversion of crotonyl-CoA to
CC butyryl-CoA. It shows a high substrate specificity for crotonyl-CoA, a
CC short-chain-length (C4), but no measurable activity is observed with
CC shorter (C3) or longer-chain-length enoyl-CoA thioesters.
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 Evidence={ECO:0000269|PubMed:8521864};
CC -!- ACTIVITY REGULATION: Inhibited by divalent cations (30-100%), beta-
CC chloromercuribenzoate (85%), iodoacetamide (40%) and N-ethylmaleamide
CC (80%). The presence of CoA thioesters containing 12-20 carbon atoms
CC results in inhibition of enzyme activity. The greatest degree of
CC inhibition is observed in the presence of palmitoyl-CoA and myristoyl-
CC CoA. The branched-chain fatty acids, isopalmitoyl-CoA and isomyristoyl-
CC CoA are less effective inhibitors of the crotonyl-CoA reductase.
CC Concentrations of NADPH above 200 uM lead to inhibition of enzyme
CC activity. {ECO:0000269|PubMed:8521864}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for crotonyl-CoA (with NADP 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 is 40 degrees Celsius.
CC {ECO:0000269|PubMed:8521864};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8521864, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Crotonyl-CoA carboxylase/reductase subfamily. {ECO:0000305}.
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DR EMBL; U37135; AAA92890.1; -; Genomic_DNA.
DR PIR; S72400; S72400.
DR PDB; 3HZZ; X-ray; 2.40 A; A/B/C/D=1-447.
DR PDBsum; 3HZZ; -.
DR AlphaFoldDB; Q53865; -.
DR SMR; Q53865; -.
DR KEGG; ag:AAA92890; -.
DR EvolutionaryTrace; Q53865; -.
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 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 3D-structure; Metal-binding; NADP; Oxidoreductase; Zinc.
FT CHAIN 1..447
FT /note="Crotonyl-CoA reductase"
FT /id="PRO_0000418532"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3HZZ"
FT TURN 39..44
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3HZZ"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:3HZZ"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:3HZZ"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:3HZZ"
FT TURN 278..282
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 353..357
FT /evidence="ECO:0007829|PDB:3HZZ"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 412..420
FT /evidence="ECO:0007829|PDB:3HZZ"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 431..441
FT /evidence="ECO:0007829|PDB:3HZZ"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:3HZZ"
SQ SEQUENCE 447 AA; 49364 MW; C275C04F80AB4A5A CRC64;
MTVKDILDAI QSKDATSADF AALQLPESYR AITVHKDETE MFAGLETRDK DPRKSIHLDE
VPVPELGPGE ALVAVMASSV NYNSVWTSIF EPVSTFAFLE RYGKLSPLTK RHDLPYHIIG
SDLAGVVLRT GPGVNAWQPG DEVVAHCLSV ELESPDGHDD TMLDPEQRIW GFETNFGGLA
EIALVKTNQL MPKPKHLTWE EAAAPGLVNS TAYRQLVSRN GAAMKQGDNV LIWGASGGLG
SYATQFALAG GANPICVVSS PQKAEICRSM GAEAIIDRNA EGYKFWKDEH TQDPKEWKRF
GKRIRELTGG EDIDIVFEHP GRETFGASVY VTRKGGTITT CASTSGYMHE YDNRYLWMSL
KRIIGSHFAN YREAYEANRL IAKGKIHPTL SKTYSLEETG QAAYDVHRNL HQGKVGVLCL
APEEGLGVRD AEMRAQHIDA INRFRNV
