BCHE_CERS4
ID BCHE_CERS4 Reviewed; 612 AA.
AC Q9RFD3; Q3J180; Q53225;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 129.
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=RHOS4_18860;
GN ORFNames=RSP_0281;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Naylor G.W., Addlesee H.A., Gibson L.C.D., Hunter C.N.;
RT "The photosynthesis gene cluster of Rhodobacter sphaeroides.";
RL Photosyn. Res. 62:121-139(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA Choudhary M., Kaplan S.;
RT "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT sphaeroides 2.4.1.";
RL Nucleic Acids Res. 28:862-867(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; AJ010302; CAB38729.1; -; Genomic_DNA.
DR EMBL; AF195122; AAF24279.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79454.1; -; Genomic_DNA.
DR PIR; T50735; T50735.
DR RefSeq; WP_011338122.1; NZ_AKVW01000001.1.
DR RefSeq; YP_353355.1; NC_007493.2.
DR AlphaFoldDB; Q9RFD3; -.
DR SMR; Q9RFD3; -.
DR STRING; 272943.RSP_0281; -.
DR EnsemblBacteria; ABA79454; ABA79454; RSP_0281.
DR GeneID; 57470599; -.
DR KEGG; rsp:RSP_0281; -.
DR PATRIC; fig|272943.9.peg.2224; -.
DR eggNOG; COG1032; Bacteria.
DR OMA; GNWPPAW; -.
DR PhylomeDB; Q9RFD3; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000002703; Chromosome 1.
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 SFLD; SFLDS00029; Radical_SAM; 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; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW Cobalamin; Cobalt; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Photosynthesis; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..612
FT /note="Anaerobic magnesium-protoporphyrin IX monomethyl
FT ester cyclase"
FT /id="PRO_0000064874"
FT DOMAIN 9..143
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT DOMAIN 190..417
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 204
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P26168"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P26168"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P26168"
FT CONFLICT 121
FT /note="V -> A (in Ref. 1; CAB38729)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="A -> P (in Ref. 1; CAB38729)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="I -> M (in Ref. 2; AAF24279)"
FT /evidence="ECO:0000305"
FT CONFLICT 518..536
FT /note="LRVQGKARAEERNAAKAEA -> ARAGQGPCRGAQCGQGRG (in Ref.
FT 1; CAB38729 and 2; AAF24279)"
FT /evidence="ECO:0000305"
FT CONFLICT 570..587
FT /note="Missing (in Ref. 1; CAB38729)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="G -> S (in Ref. 2; AAF24279)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 69219 MW; D461626D4B722CF3 CRC64;
MRIVFVHPNY HSGGAEIAGS WPPAWVAYLC GALKKAGYTD YHFIDAMTDY VSHEKLAEKL
RELQPDIVAT TAITPSIYVA EETLKVAMEV VPNALRVLGG IHATFMFRQV LEEAPWIDVI
VRGEGEEVLV NLVKAYEADN FAETRRQVKG LAFLDGDEIV STAAAPTIRD VDSIDPDWGI
INWKNYIYEP LGVRVAIPNM ARGCPFTCSF CSQWKFWRDY RVRDPKKVVD EIEKLVNEHG
VGFFILADEE PTINRKKFIE FCEEMIARGL PDKVKWGINT RVTDVKRDKE LLKFYRKAGL
VHISLGTEAA AQLKLDVFNK ETTVAENKEA IRLLREADIF TEAQFIVGLD NETKETLEET
YRMAWDWQPD LANWSMYTPW PFTPLFQELR DQVEVFDYSK YNFVTPIMKP KALTRGELLD
GVMNNYRRFY MKKALFHYPW RGTGFRRRYL LGCLKAFLKA GVGRTFYDLG KAGYWGPQSK
DKVDFHFDET RKIGNAQMAD WEASADRAAK AAERREALRV QGKARAEERN AAKAEAAPIL
TAGGGGCGGH ADGSDCGCGG KKQQQVDEFH VPMACGGGRQ QMAEDEFAMP MACGGGKQQM
EEAEERLVRP AE
