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BCHE_SYNY3
ID   BCHE_SYNY3              Reviewed;         499 AA.
AC   Q55373;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase {ECO:0000250|UniProtKB:P26168};
DE            Short=MPE cyclase {ECO:0000250|UniProtKB:P26168};
DE            EC=1.21.98.3 {ECO:0000250|UniProtKB:P26168};
GN   Name=bchE {ECO:0000250|UniProtKB:P26168}; OrderedLocusNames=slr0905;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Involved in the tetrapyrrole biosynthetic pathways leading to
CC       chlorophyll and bacteriochlorophyll (BChl). Catalyzes the anaerobic
CC       formation of the isocyclic ring (E-ring) in Mg-protoporphyrin
CC       monomethyl ester (MPE) to yield protochlorophyllide a (PChlide a) via a
CC       six-electron oxidation and the formation of an oxo group at position
CC       C13 using oxygen from a water molecule. {ECO:0000250|UniProtKB:P26168}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + Mg-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-
CC         L-methionine = 3,8-divinyl protochlorophyllide a + 3 5'-
CC         deoxyadenosine + 4 H(+) + 3 L-methionine; Xref=Rhea:RHEA:49096,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:58632, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:60491; EC=1.21.98.3;
CC         Evidence={ECO:0000250|UniProtKB:P26168};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P26168};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P26168};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000250|UniProtKB:P26168};
CC       Note=Binds 1 adenosylcobalamin. {ECO:0000250|UniProtKB:P26168};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC       biosynthesis (light-independent). {ECO:0000250|UniProtKB:P26168}.
CC   -!- SIMILARITY: Belongs to the BchE family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA10457.1; -; Genomic_DNA.
DR   PIR; S75722; S75722.
DR   AlphaFoldDB; Q55373; -.
DR   SMR; Q55373; -.
DR   IntAct; Q55373; 1.
DR   STRING; 1148.1001215; -.
DR   PaxDb; Q55373; -.
DR   EnsemblBacteria; BAA10457; BAA10457; BAA10457.
DR   KEGG; syn:slr0905; -.
DR   eggNOG; COG1032; Bacteria.
DR   InParanoid; Q55373; -.
DR   PhylomeDB; Q55373; -.
DR   UniPathway; UPA00671; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR034466; Methyltransferase_Class_B.
DR   InterPro; IPR007197; rSAM.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR   SMART; SM00729; Elp3; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Chlorophyll biosynthesis; Cobalamin; Cobalt; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Photosynthesis; Reference proteome;
KW   S-adenosyl-L-methionine.
FT   CHAIN           1..499
FT                   /note="Anaerobic magnesium-protoporphyrin IX monomethyl
FT                   ester cyclase"
FT                   /id="PRO_0000064875"
FT   DOMAIN          9..145
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   DOMAIN          188..420
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         202
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P26168"
FT   BINDING         206
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P26168"
FT   BINDING         209
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P26168"
SQ   SEQUENCE   499 AA;  57793 MW;  A0E094812D85C285 CRC64;
     MRILILNPPH PAIGSRIPKE QLPPLGLLSI GGPLLDAGHD VTLLDAEFGP LTDSEIVERV
     CAHCPQLLLI GHSGSTSAHP IVCRLTLFLR ERLPNLIIVY GGVFPTYHFH DILTKEPQID
     FIVRGEGEAT VAKLIAALEN HNDLNKVDGI AFRRDEQIIE TLPAPMIQDL DVYRVGWELV
     DLKKYSYYGG KQAVVIQFSR GCPHLCNYCG QRGFWARWRH RDPKKFAQEI VWLHRTHGVQ
     LFNLADENPT VNKAIWQEFC EAIIAENISI TIIGSTRADD IVRDADILHL YRRAGVERFL
     LGMENTNEAT LKHIRKGSKT STDREAIRLL RQHNILSLAT WVTDFEEVRD RDFIQALKQL
     LYYDPDQIMS LYVTPHRWTS FYGIASERRV IQLDQTKWDY KHQVLAATHM PPWRIFLWVK
     LIEILLQTRP KALWRLLFQP NKASRRGMYW FTLMGRRVLV HELINFFFGD RRVKNGPTLQ
     EFWGMPQEHQ EIPLSITRK
 
 
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