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HEM4_ARATH
ID   HEM4_ARATH              Reviewed;         321 AA.
AC   O48721; Q8LBE8; Q8RVZ2; Q8VZ12;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Uroporphyrinogen-III synthase, chloroplastic {ECO:0000303|PubMed:18042043};
DE            Short=AtUROS {ECO:0000303|PubMed:18042043};
DE            EC=4.2.1.75 {ECO:0000269|PubMed:18042043};
DE   AltName: Full=Hydroxymethylbilane hydrolyase [cyclizing] {ECO:0000303|PubMed:18042043};
DE   AltName: Full=Uroporphyrinogen-III cosynthase {ECO:0000303|PubMed:18042043};
DE   Flags: Precursor;
GN   Name=UROS {ECO:0000303|PubMed:18042043};
GN   Synonyms=HEMD {ECO:0000303|PubMed:18042043};
GN   OrderedLocusNames=At2g26540 {ECO:0000312|Araport:AT2G26540};
GN   ORFNames=T9J22.21 {ECO:0000312|EMBL:AAC14502.2};
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], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=18042043; DOI=10.1042/bj20070770;
RA   Tan F.-C., Cheng Q., Saha K., Heinemann I.U., Jahn M., Jahn D., Smith A.G.;
RT   "Identification and characterization of the Arabidopsis gene encoding the
RT   tetrapyrrole biosynthesis enzyme uroporphyrinogen III synthase.";
RL   Biochem. J. 410:291-299(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-321.
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Catalyzes cyclization of the linear tetrapyrrole,
CC       hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, a
CC       precursor of tetrapyrroles such as chlorophyll, heme and phycobilins.
CC       {ECO:0000269|PubMed:18042043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydroxymethylbilane = H2O + uroporphyrinogen III;
CC         Xref=Rhea:RHEA:18965, ChEBI:CHEBI:15377, ChEBI:CHEBI:57308,
CC         ChEBI:CHEBI:57845; EC=4.2.1.75;
CC         Evidence={ECO:0000269|PubMed:18042043};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
CC       {ECO:0000269|PubMed:18042043}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis. {ECO:0000269|PubMed:18042043}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:18042043}.
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen-III synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ314569; CAC85287.1; -; mRNA.
DR   EMBL; AC002505; AAC14502.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07854.1; -; Genomic_DNA.
DR   EMBL; BT026116; ABG48472.1; -; mRNA.
DR   EMBL; AY087255; AAM64811.1; -; mRNA.
DR   EMBL; AY065389; AAL38830.2; -; mRNA.
DR   PIR; T00987; T00987.
DR   RefSeq; NP_565625.1; NM_128211.4.
DR   AlphaFoldDB; O48721; -.
DR   SMR; O48721; -.
DR   BioGRID; 2547; 1.
DR   STRING; 3702.AT2G26540.1; -.
DR   iPTMnet; O48721; -.
DR   PaxDb; O48721; -.
DR   PRIDE; O48721; -.
DR   ProteomicsDB; 230185; -.
DR   EnsemblPlants; AT2G26540.1; AT2G26540.1; AT2G26540.
DR   GeneID; 817195; -.
DR   Gramene; AT2G26540.1; AT2G26540.1; AT2G26540.
DR   KEGG; ath:AT2G26540; -.
DR   Araport; AT2G26540; -.
DR   TAIR; locus:2066256; AT2G26540.
DR   eggNOG; ENOG502QST9; Eukaryota.
DR   HOGENOM; CLU_011276_9_2_1; -.
DR   InParanoid; O48721; -.
DR   OMA; LRNVYYP; -.
DR   OrthoDB; 1423947at2759; -.
DR   PhylomeDB; O48721; -.
DR   BioCyc; ARA:AT2G26540-MON; -.
DR   BioCyc; MetaCyc:AT2G26540-MON; -.
DR   BRENDA; 4.2.1.75; 399.
DR   UniPathway; UPA00251; UER00320.
DR   UniPathway; UPA00668; -.
DR   PRO; PR:O48721; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O48721; baseline and differential.
DR   Genevisible; O48721; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR   GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IDA:UniProtKB.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006780; P:uroporphyrinogen III biosynthetic process; IDA:UniProtKB.
DR   CDD; cd06578; HemD; 1.
DR   Gene3D; 3.40.50.10090; -; 2.
DR   InterPro; IPR036108; 4pyrrol_syn_uPrphyn_synt_sf.
DR   InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth.
DR   InterPro; IPR039793; UROS/Hem4.
DR   PANTHER; PTHR38042; PTHR38042; 1.
DR   Pfam; PF02602; HEM4; 1.
DR   SUPFAM; SSF69618; SSF69618; 1.
PE   1: Evidence at protein level;
KW   Chlorophyll biosynthesis; Chloroplast; Lyase; Plastid;
KW   Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..81
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           82..321
FT                   /note="Uroporphyrinogen-III synthase, chloroplastic"
FT                   /id="PRO_0000376067"
FT   CONFLICT        29
FT                   /note="I -> V (in Ref. 1; CAC85287)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="V -> I (in Ref. 5; AAM64811)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   321 AA;  34225 MW;  747E4E3C2DCEBD08 CRC64;
     MALLLLSHCS ILSFQPPLSS SSSFHSSHIQ SLSKPVFASP SPIRNSISSS VSSSSSSVSS
     SNSIPQVVVT RERGKNNQII KALEKNGISS LELPLIQHAR GPDFDRLASV LNDKSFDWII
     ITSPEAGSVF LEAWKTASSP EVQIGVVGAG TARVFEEAMK SADGLLHVAF TPSKATGKVL
     ASELPEKVGK RSSVLYPASL KAGNDIVEGL SKRGFEVVRL NTYTTVPVQS VDTVLLQQAL
     SAPVLSVASP SAVRAWLHLI QNEEQWSNYV ACIGETTASA ARRLGLKNVY YPEKPGLEGW
     VESIMEALGA HADSSNPSSR N
 
 
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