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AAE4_ARATH
ID   AAE4_ARATH              Reviewed;         545 AA.
AC   O80658; Q8LRT5;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Probable acyl-activating enzyme 4;
DE            EC=6.2.1.-;
DE   AltName: Full=AMP-binding protein 4;
DE            Short=AtAMPBP4;
GN   Name=AEE4; Synonyms=AMPBP4; OrderedLocusNames=At1g77240; ORFNames=T14N5.10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12177484; DOI=10.1104/pp.003269;
RA   Shockey J.M., Fulda M.S., Browse J.A.;
RT   "Arabidopsis contains nine long-chain acyl-coenzyme A synthetase genes that
RT   participate in fatty acid and glycerolipid metabolism.";
RL   Plant Physiol. 129:1710-1722(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12805634; DOI=10.1104/pp.103.020552;
RA   Shockey J.M., Fulda M.S., Browse J.;
RT   "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT   Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme
RT   a synthetases.";
RL   Plant Physiol. 132:1065-1076(2003).
CC   -!- FUNCTION: May act as an acid--thiol ligase that activates carboxylic
CC       acids by forming acyl-CoAs. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC       developing seeds. {ECO:0000269|PubMed:12805634}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AF503763; AAM28621.1; -; mRNA.
DR   EMBL; AC004260; AAC34346.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35953.1; -; Genomic_DNA.
DR   PIR; T00453; T00453.
DR   RefSeq; NP_177848.1; NM_106373.2.
DR   AlphaFoldDB; O80658; -.
DR   SMR; O80658; -.
DR   STRING; 3702.AT1G77240.1; -.
DR   PaxDb; O80658; -.
DR   PRIDE; O80658; -.
DR   ProteomicsDB; 245091; -.
DR   EnsemblPlants; AT1G77240.1; AT1G77240.1; AT1G77240.
DR   GeneID; 844060; -.
DR   Gramene; AT1G77240.1; AT1G77240.1; AT1G77240.
DR   KEGG; ath:AT1G77240; -.
DR   Araport; AT1G77240; -.
DR   TAIR; locus:2195950; AT1G77240.
DR   eggNOG; KOG1176; Eukaryota.
DR   HOGENOM; CLU_000022_59_5_1; -.
DR   InParanoid; O80658; -.
DR   OMA; EDGDPKF; -.
DR   OrthoDB; 312083at2759; -.
DR   PhylomeDB; O80658; -.
DR   PRO; PR:O80658; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O80658; differential.
DR   Genevisible; O80658; AT.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   Fatty acid metabolism; Ligase; Lipid metabolism; Reference proteome.
FT   CHAIN           1..545
FT                   /note="Probable acyl-activating enzyme 4"
FT                   /id="PRO_0000415715"
FT   CONFLICT        123
FT                   /note="S -> L (in Ref. 1; AAM28621)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   545 AA;  60011 MW;  22CF3108903E6669 CRC64;
     MELLLPHASN SCPLTVLGFL ERAASVFGDS PSLLHTTTVH TWSETHSRCL RIASTLSSAS
     LGINRGQVVS VIGPNVPSVY ELQFAVPMSG AVLNNINPRL DAHALSVLLR HSESKLVFVD
     HHSSSLVLEA VSFLPKDERP RLVILNDGND MPSSSSADMD FLDTYEGFME RGDLRFKWVR
     PKSEWTPMVL NYTSGTTSSP KGVVHSHRSV FMSTINSLLD WSLPNRPVYL WTLPMFHANG
     WSYTWATAAV GARNICVTRV DVPTIFNLID KYQVTHMCAA PMVLNMLTNH PAQKPLQSPV
     KVMTAGAPPP ATVISKAEAL GFDVSHGYGM TETGGLVVSC ALKPEWDRLE PDERAKQKSR
     QGIRTAVFAE VDVRDPISGK SVKHDGATVG EIVFRGGSVM LGYYKDPEGT AASMREDGWF
     YTGDIGVMHP DGYLEVKDRS KDVVICGGEN ISSTELEAVL YTNPAIKEAA VVAKPDKMWG
     ETPCAFVSLK YHDGSVTERE IREFCKTKLP KYMVPRNVVF LEELPKTSTG KIQKFLLRQM
     AKSLP
 
 
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