BCHE_RUBGE
ID BCHE_RUBGE Reviewed; 555 AA.
AC Q7X2C7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase {ECO:0000303|PubMed:14617630};
DE Short=MPE cyclase {ECO:0000303|PubMed:14617630};
DE EC=1.21.98.3 {ECO:0000305|PubMed:14617630};
GN Name=bchE;
OS Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas
OS gelatinosa).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX NCBI_TaxID=28068;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=14617630; DOI=10.1074/jbc.m309851200;
RA Ouchane S., Steunou A.-S., Picaud M., Astier C.;
RT "Aerobic and anaerobic Mg-protoporphyrin monomethyl ester cyclases in
RT purple bacteria: a strategy adopted to bypass the repressive oxygen control
RT system.";
RL J. Biol. Chem. 279:6385-6394(2004).
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:0000269|PubMed:14617630}.
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:0000305|PubMed:14617630};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:14617630};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:14617630};
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:0000305|PubMed:14617630}.
CC -!- DISRUPTION PHENOTYPE: Cells do not exhibit a phenotype under high-
CC aeration respiratory growth conditions. In contrast, under low-aerated
CC respiratory growth conditions, the absence of BchE leads to an
CC accumulation of MgPMME. {ECO:0000269|PubMed:14617630}.
CC -!- SIMILARITY: Belongs to the BchE family. {ECO:0000305}.
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DR EMBL; AY309082; AAP73428.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7X2C7; -.
DR SMR; Q7X2C7; -.
DR BRENDA; 1.21.98.3; 5401.
DR UniPathway; UPA00671; -.
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; 3.80.30.20; -; 1.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR034466; Methyltransferase_Class_B.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
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 1: Evidence at protein level;
KW 4Fe-4S; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW Cobalamin; Cobalt; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Photosynthesis; S-adenosyl-L-methionine.
FT CHAIN 1..555
FT /note="Anaerobic magnesium-protoporphyrin IX monomethyl
FT ester cyclase"
FT /id="PRO_0000064873"
FT DOMAIN 9..143
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT DOMAIN 191..416
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 205
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305|PubMed:14617630"
FT BINDING 209
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305|PubMed:14617630"
FT BINDING 212
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305|PubMed:14617630"
SQ SEQUENCE 555 AA; 63536 MW; 0A01B0E9E9F8C2B5 CRC64;
MRVLFIHPNY HSGGAEIAGN WPPAWVAYLA GYLKAGGYTD VIFVDAMTND LSEDQVREKI
TTLKPDIVGC TAITPAIYKA ERTLQIAKEV NPDIVTVLGG IHGTFMYPQV LKEAPWIDAI
VRGEGEQVML NLVTAVDQGR FMADRNCVNG IAYAAPDGKV VATPAEPPIE DLDRITPDWG
ILEWEKYIYI PMNKRVAIPN FARGCPFTCS FCSQWKFWRD YRIRDPKKVV DEIEVLVKQH
DVGFFILADE EPTIHRKKFI EFCEELIKRD LGVLWGINTR VTDILRDEKL LPLFRKAGLI
HVSLGTEAAA QLKLDMVNKE TTIEQNKRAI QLLKDNGIVT EAQFIVGLEN ETAETLEETY
KMARDWNPDM ANWAMYTPWP FSDLFQELGD KVEVFDFEKY NFVTPIMKPD AMDRGELLDR
VMSNYRRFFM NKAFLQYPFT KDKERRKYLM GCLKAFLKSG FERKFYDLGR VGYWGPQTKK
TVNFSFDKNR RIDAQTADEL SRVDDGWVTM HGPKIEMRRR KGDDNFEIAK AAMACGGGTE
QLTEEQQAAT EVRAS
