BCHE_RHOCB
ID BCHE_RHOCB Reviewed; 575 AA.
AC P26168; D5ANT0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase {ECO:0000303|PubMed:10841582};
DE Short=MPE cyclase {ECO:0000303|PubMed:10841582};
DE EC=1.21.98.3 {ECO:0000269|PubMed:10841582};
GN Name=bchE {ECO:0000303|PubMed:8385667}; OrderedLocusNames=RCAP_rcc00669;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=8385667; DOI=10.1128/jb.175.8.2414-2422.1993;
RA Burke D.H., Alberti M., Hearst J.E.;
RT "bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus and
RT identification of the third subunit of light-independent
RT protochlorophyllide reductase in bacteria and plants.";
RL J. Bacteriol. 175:2414-2422(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [3]
RP FUNCTION, AND PATHWAY.
RX PubMed=2203738; DOI=10.1128/jb.172.9.5001-5010.1990;
RA Yang Z.M., Bauer C.E.;
RT "Rhodobacter capsulatus genes involved in early steps of the
RT bacteriochlorophyll biosynthetic pathway.";
RL J. Bacteriol. 172:5001-5010(1990).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=37b4;
RX PubMed=10841582; DOI=10.1073/pnas.97.12.6908;
RA Gough S.P., Petersen B.O., Duus J.O.;
RT "Anaerobic chlorophyll isocyclic ring formation in Rhodobacter capsulatus
RT requires a cobalamin cofactor.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6908-6913(2000).
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:10841582,
CC ECO:0000305|PubMed:2203738}.
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:0000269|PubMed:10841582};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:10841582};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305|PubMed:10841582};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000269|PubMed:10841582};
CC Note=Binds 1 adenosylcobalamin. {ECO:0000269|PubMed:10841582};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis (light-independent). {ECO:0000305|PubMed:2203738}.
CC -!- SIMILARITY: Belongs to the BchE family. {ECO:0000305}.
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DR EMBL; Z11165; CAA77530.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84434.1; -; Genomic_DNA.
DR PIR; S17814; S17814.
DR RefSeq; WP_013066413.1; NC_014034.1.
DR AlphaFoldDB; P26168; -.
DR SMR; P26168; -.
DR STRING; 272942.RCAP_rcc00669; -.
DR PRIDE; P26168; -.
DR EnsemblBacteria; ADE84434; ADE84434; RCAP_rcc00669.
DR GeneID; 31489615; -.
DR KEGG; rcp:RCAP_rcc00669; -.
DR eggNOG; COG1032; Bacteria.
DR HOGENOM; CLU_021572_4_0_5; -.
DR OMA; GNWPPAW; -.
DR OrthoDB; 973846at2; -.
DR BioCyc; MetaCyc:MON-13265; -.
DR BRENDA; 1.21.98.3; 5381.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000002361; 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:0030494; P:bacteriochlorophyll biosynthetic process; IMP:CACAO.
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; IPR036724; Cobalamin-bd_sf.
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 SUPFAM; SSF52242; SSF52242; 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; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..575
FT /note="Anaerobic magnesium-protoporphyrin IX monomethyl
FT ester cyclase"
FT /id="PRO_0000064872"
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 REGION 504..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 204
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305|PubMed:10841582"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305|PubMed:10841582"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305|PubMed:10841582"
SQ SEQUENCE 575 AA; 65866 MW; A1814FBF9D877310 CRC64;
MRILFVHPNY HSGGAEIAGN WPPSWVPYLA GHLKKAGFDD IHFIDAMTLN VSHDELRKKF
AELQPDLIGV TSITPSIYEA EETLKIAKEV VPNAVRVLGG VHATFMFRQV LSEAPWVDAI
VRGEGEEIMV ELAKCVSEGR WPEDRASIKG LAFHDGTEIV ATQAAPTVKD IDSLKPDWSL
IDWKHYIYIP LGVRVAIPNM ARGCPFTCSF CSQWKFWRDY RVRSPKAVVD EIEDLVNNYD
VGFFILADEE PTINKKKFVE FCQEMIDRGL NHKVKWGINT RVTDIYRDRD LLKFYREAGL
VHISLGTEAA AQLKLDLFNK ETTVAENKEA IRLLREADIF TEAQFIVGLD NETKETLEET
FQMAWDWQPD LANWSMYTPW PFTPLFQELR DQVEVFDFSK YNFVTPIMKP KALTRGELLD
GVMKNYRRFY MRKALFHYPW RGTGFRRRYL LGCLKAFLKA GVGRTFYDLG KAGYWGPQTK
DTVDFHFDET RKIAEAQVAD WEAAADRSRK HKERQEALRA QMKDRAADRN TANFVMPADA
EDEFDLSAET HEARSAEHAA MACGGGKDQM VDAAE
