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 27-MAR-2024, entry version 143.
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; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC 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.gene:10499958; -.
DR PaxDb; 1148-1001215; -.
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 CDD; cd02068; radical_SAM_B12_BD; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034466; Methyltransferase_Class_B.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR02026; BchE; 1.
DR PANTHER; PTHR43409:SF7; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE; 1.
DR PANTHER; PTHR43409; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE-RELATED; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 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
//
