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CRD1_CHLRE
ID   CRD1_CHLRE              Reviewed;         407 AA.
AC   Q9LD46;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 1, chloroplastic;
DE            Short=Mg-protoporphyrin IX monomethyl ester oxidative cyclase 1;
DE            EC=1.14.13.81;
DE   AltName: Full=Copper response defect 1 protein;
DE   AltName: Full=Copper-response target 1 protein;
DE   Flags: Precursor;
GN   Name=CRD1;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX   PubMed=10811605; DOI=10.1093/emboj/19.10.2139;
RA   Moseley J.L., Quinn J., Eriksson M., Merchant S.;
RT   "The Crd1 gene encodes a putative di-iron enzyme required for photosystem I
RT   accumulation in copper deficiency and hypoxia in Chlamydomonas
RT   reinhardtii.";
RL   EMBO J. 19:2139-2151(2000).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12485992; DOI=10.1093/emboj/cdf666;
RA   Moseley J.L., Allinger T., Herzog S., Hoerth P., Wehinger E., Merchant S.,
RA   Hippler M.;
RT   "Adaptation to Fe-deficiency requires remodeling of the photosynthetic
RT   apparatus.";
RL   EMBO J. 21:6709-6720(2002).
RN   [3]
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=11910013; DOI=10.1105/tpc.010420;
RA   Moseley J.L., Page M.D., Alder N.P., Eriksson M., Quinn J., Soto F.,
RA   Theg S.M., Hippler M., Merchant S.;
RT   "Reciprocal expression of two candidate di-iron enzymes affecting
RT   photosystem I and light-harvesting complex accumulation.";
RL   Plant Cell 14:673-688(2002).
RN   [4]
RP   INDUCTION.
RX   PubMed=11842150; DOI=10.1104/pp.010694;
RA   Quinn J.M., Eriksson M., Moseley J.L., Merchant S.;
RT   "Oxygen deficiency responsive gene expression in Chlamydomonas reinhardtii
RT   through a copper-sensing signal transduction pathway.";
RL   Plant Physiol. 128:463-471(2002).
CC   -!- FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll
CC       biosynthesis under oxygen- and copper-deficient conditions. Mediates
CC       the cyclase reaction, which results in the formation of
CC       divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls
CC       from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME).
CC       {ECO:0000269|PubMed:10811605, ECO:0000269|PubMed:12485992}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + Mg-protoporphyrin IX 13-monomethyl ester + 3 NADPH +
CC         3 O2 = 3,8-divinyl protochlorophyllide a + 5 H2O + 3 NADP(+);
CC         Xref=Rhea:RHEA:33235, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58632, ChEBI:CHEBI:60491; EC=1.14.13.81;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:11910013, ECO:0000269|PubMed:12485992}.
CC   -!- INDUCTION: Induced in absence of copper and oxygen. Regulated by CRR1
CC       protein, which activates its transcription in absence of copper.
CC       {ECO:0000269|PubMed:10811605, ECO:0000269|PubMed:11842150,
CC       ECO:0000269|PubMed:11910013}.
CC   -!- SIMILARITY: Belongs to the AcsF family. {ECO:0000305}.
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DR   EMBL; AF226628; AAF65221.1; -; Genomic_DNA.
DR   EMBL; AF237671; AAF63477.1; -; mRNA.
DR   RefSeq; XP_001692557.1; XM_001692505.1.
DR   AlphaFoldDB; Q9LD46; -.
DR   SMR; Q9LD46; -.
DR   STRING; 3055.EDP04035; -.
DR   DNASU; 5718021; -.
DR   EnsemblPlants; PNW81190; PNW81190; CHLRE_07g346050v5.
DR   EnsemblPlants; PNW81191; PNW81191; CHLRE_07g346050v5.
DR   GeneID; 5718021; -.
DR   Gramene; PNW81190; PNW81190; CHLRE_07g346050v5.
DR   Gramene; PNW81191; PNW81191; CHLRE_07g346050v5.
DR   KEGG; cre:CHLRE_07g346050v5; -.
DR   eggNOG; ENOG502QRIH; Eukaryota.
DR   HOGENOM; CLU_048037_0_0_1; -.
DR   OMA; EMFLLMS; -.
DR   OrthoDB; 930662at2759; -.
DR   BRENDA; 1.14.13.81; 1318.
DR   UniPathway; UPA00668; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048529; F:magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   CDD; cd01047; ACSF; 1.
DR   HAMAP; MF_01840; AcsF; 1.
DR   InterPro; IPR008434; AcsF.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR003251; Rubrerythrin.
DR   PANTHER; PTHR31053; PTHR31053; 1.
DR   Pfam; PF02915; Rubrerythrin; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
DR   TIGRFAMs; TIGR02029; AcsF; 1.
PE   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Chloroplast; Iron; Membrane; Metal-binding; NADP;
KW   Oxidoreductase; Photosynthesis; Plastid; Thylakoid; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..407
FT                   /note="Magnesium-protoporphyrin IX monomethyl ester
FT                   [oxidative] cyclase 1, chloroplastic"
FT                   /id="PRO_0000000599"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   407 AA;  47212 MW;  FD13EE5AC9C55CFE CRC64;
     MQTTLKQQRA SGRVSARQPF RSAAVARPRR STVRVQASAA PLNDGLGFET MRDGIKVAAK
     ETLLTPRFYT TDFDEMEQLF SKEINPNLDM EELNACLNEF RNDYNKVHFV RNETFKAAAD
     KVTGETRRIF IEFLERSCTA EFSGFLLYKE LARRMKASSP EVAEMFLLMS RDEARHAGFL
     NKALSDFNLA LDLGFLTKNR TYTYFKPKFI IYATFLSEKI GYWRYITIYR HLQRNPDNQF
     YPLFEYFENW CQDENRHGDF LAACLKAKPE LLNTFEAKLW SKFFCLSVYI TMYLNDHQRT
     KFYESLGLNT RQFNQHVIIE TNRATERLFP VVPDVEDPRF FEILNKMVDV NAKLVELSAS
     SSPLAGLQKL PLLERMASYC LQLLFFKEKD VGSVDIAGSG ASRNLAY
 
 
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