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4CL2_DICDI
ID   4CL2_DICDI              Reviewed;         551 AA.
AC   Q54P78;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Probable 4-coumarate--CoA ligase 2;
DE            Short=4CL 2;
DE            EC=6.2.1.12;
DE   AltName: Full=4-coumaroyl-CoA synthase 2;
GN   Name=4cl2; ORFNames=DDB_G0284745;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:19641, ChEBI:CHEBI:12876,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:85008, ChEBI:CHEBI:456215; EC=6.2.1.12;
CC   -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene
CC       biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step
CC       1/2.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000071; EAL65025.1; -; Genomic_DNA.
DR   RefSeq; XP_638380.1; XM_633288.1.
DR   AlphaFoldDB; Q54P78; -.
DR   SMR; Q54P78; -.
DR   STRING; 44689.DDB0231736; -.
DR   PaxDb; Q54P78; -.
DR   EnsemblProtists; EAL65025; EAL65025; DDB_G0284745.
DR   GeneID; 8624749; -.
DR   KEGG; ddi:DDB_G0284745; -.
DR   dictyBase; DDB_G0284745; 4cl2.
DR   eggNOG; KOG1176; Eukaryota.
DR   HOGENOM; CLU_000022_59_2_1; -.
DR   InParanoid; Q54P78; -.
DR   OMA; WLMQRAF; -.
DR   PhylomeDB; Q54P78; -.
DR   UniPathway; UPA00372; UER00547.
DR   PRO; PR:Q54P78; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Phenylpropanoid metabolism;
KW   Reference proteome.
FT   CHAIN           1..551
FT                   /note="Probable 4-coumarate--CoA ligase 2"
FT                   /id="PRO_0000327702"
SQ   SEQUENCE   551 AA;  61149 MW;  D67106EBB8D79D2C CRC64;
     MIRMIKGQIY FTSKYPNIII PEKPIPHLIL KHIRSKPDQV LLVDGLTFKE YSSHFVADTI
     EKVACGLNKL NIKKGDVLGV ILPNLPEYVP IFHGTLLMGG ITSLVNPDYT IEELSHTLAT
     VSPRYLAVTL AVYEKIKNDL KRVFPSVEKV ILVDIAGQTL KEIGQLTLSS DGIVMSFNQL
     INNNGKDYPI VRIDLKKDTA IIPFSSGTTG LFKGVCLSHH NLVSNTHQTQ TVETTNYKKN
     DTVMGQLPFF HIYGLMTYLI LMVKQGHCVV ILPKFEFVRF LDLIQKYKVA ISFIVPPIAI
     MFAKSPIVDK FDLSSLRTLF SGAAPLSREV EDLIKERFKG KLIIKQGYGA TELSPACFVI
     PSGLIKSGSA GILLPNQLVK IISPETGENL GMGEKGEICI KGPNVMLGYY NNEKATNEVI
     DKDGFFKTGD IGYVDEDGYY FIVDRSKELI KCKGFQVPPA ELEALLLSHP KVADACVVGL
     SKGDMGEVPR GFVVIKQNES LTEKELLDWA HPKIANYKHF RGGIFFIPAI PKSATGKLLR
     KNLKDINPPK L
 
 
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