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SPE1_ORYSJ
ID   SPE1_ORYSJ              Reviewed;         702 AA.
AC   Q9SNN0; A0A0P0WSJ3; A9YLB8; Q0DEW4; Q6J285;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Arginine decarboxylase 1;
DE            Short=ARGDC1;
DE            Short=OsADC1;
DE            EC=4.1.1.19;
GN   Name=ADC1; OrderedLocusNames=Os06g0131300, LOC_Os06g04070;
GN   ORFNames=P0493C11.18;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=16769152; DOI=10.1016/j.jplph.2006.04.006;
RA   Akiyama T., Jin S.;
RT   "Molecular cloning and characterization of an arginine decarboxylase gene
RT   up-regulated by chilling stress in rice seedlings.";
RL   J. Plant Physiol. 164:645-654(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Eyi 105;
RX   PubMed=20082138; DOI=10.1007/s11248-009-9354-0;
RA   Peremarti A., Bassie L., Zhu C., Christou P., Capell T.;
RT   "Molecular characterization of the Arginine decarboxylase gene family in
RT   rice.";
RL   Transgenic Res. 19:785-797(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:58145; EC=4.1.1.19;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems (at protein
CC       level). {ECO:0000269|PubMed:16769152, ECO:0000269|PubMed:20082138}.
CC   -!- INDUCTION: By cold stress. {ECO:0000269|PubMed:16769152}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000305}.
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DR   EMBL; AY604047; AAT37534.1; -; mRNA.
DR   EMBL; EU220429; ABY47890.1; -; mRNA.
DR   EMBL; AP000559; BAA84799.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF18609.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS95983.1; -; Genomic_DNA.
DR   RefSeq; XP_015643038.1; XM_015787552.1.
DR   AlphaFoldDB; Q9SNN0; -.
DR   SMR; Q9SNN0; -.
DR   STRING; 4530.OS06T0131300-00; -.
DR   PaxDb; Q9SNN0; -.
DR   PRIDE; Q9SNN0; -.
DR   EnsemblPlants; Os06t0131300-01; Os06t0131300-01; Os06g0131300.
DR   GeneID; 4340008; -.
DR   Gramene; Os06t0131300-01; Os06t0131300-01; Os06g0131300.
DR   KEGG; osa:4340008; -.
DR   eggNOG; ENOG502QTXD; Eukaryota.
DR   HOGENOM; CLU_027243_0_0_1; -.
DR   InParanoid; Q9SNN0; -.
DR   OMA; AVEYTQH; -.
DR   OrthoDB; 762520at2759; -.
DR   BRENDA; 4.1.1.19; 4460.
DR   PlantReactome; R-OSA-1119304; Putrescine biosynthesis II.
DR   PlantReactome; R-OSA-1119447; Putrescine biosynthesis I.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
DR   GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06830; PLPDE_III_ADC; 1.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR43295; PTHR43295; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   PIRSF; PIRSF001336; Arg_decrbxlase; 1.
DR   PRINTS; PR01180; ARGDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR01273; speA; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Lyase; Magnesium; Putrescine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..702
FT                   /note="Arginine decarboxylase 1"
FT                   /id="PRO_0000149952"
FT   REGION          668..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         336..346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         151
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        235
FT                   /note="V -> M (in Ref. 2; ABY47890)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   702 AA;  74064 MW;  3B6B8E7AF4959126 CRC64;
     MPALAVDAAA PVAHAFACDA ARFPAPLLGP AAAAAAVAEK PDAAAWSADL SSALYNVDGW
     GAPYFFVNDD GDVAVRPHGA ATLPGQEIDL AKVVAKAAGP RSGGGLGLPL PLLVRFPDVL
     RHRVEALNAA FDYAVRSTGY GGRYQGVYPV KCNQDRHVVE DIVEFGEPFR FGLEAGSKPE
     LLLAMSCLAA RGNPDALLIC NGYKDDEYVS LALIARTMGL NTVIVLEQEE ELDIVVDASR
     RLGVRPVVGM RAKLRTKHAG HFGSTSGEKG KFGLNAAQIL SVVAKLKTLG MLDCLQLLHF
     HIGSQIPTTA LLGDGVGEAA QIYCELARLG AAMRVIDVGG GLGIDYDGSH SAQTDMSVAY
     SLEEYAAAVV AAVGRVCDRK GVAHPIICSE SGRALVSHHS VLVFEAFSAS APGRIDPATG
     YLLDELTDDC HADYRNLMAA AVRGDFDTCA LYADQLKRRC ADQFKDGVLG LEHLAAVDSL
     CEIVARGMGA AEPPRTYHIN LSVFTSLPDM WAIGQMFPII PIQRLGERPA VDGVLSDLTC
     DSDGKVDHFI GGRHSLPLHE LPVHGTRGYY LGMFLGGAYQ EALGGLHNLF GGPSVVRVSQ
     SDGPHCFAVT RAAAGPSCAD VLRSMQHEPE VMFEVLKQRT DGATAAALAR AFGAMPYLSF
     DPEAAAMASG ESSGMSSDSE GSAAGAAEED DDEWEFMRGL TV
 
 
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