BCID_CHLLM
ID BCID_CHLLM Reviewed; 402 AA.
AC N0DKX5;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Bacteriochlorophyllide c C-7(1)-hydroxylase;
DE EC=1.17.98.2 {ECO:0000269|PubMed:27994052};
DE AltName: Full=Radical S-adenosyl-L-methionine (SAM) enzyme BciD {ECO:0000303|PubMed:27994052};
GN Name=bciD {ECO:0000303|PubMed:23560066};
GN ORFNames=BIU88_11010 {ECO:0000312|EMBL:AOS84617.1};
OS Chlorobaculum limnaeum.
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=274537;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=RK-j-1 {ECO:0000312|EMBL:BAN14903.1};
RX PubMed=23560066; DOI=10.1371/journal.pone.0060026;
RA Harada J., Mizoguchi T., Satoh S., Tsukatani Y., Yokono M., Noguchi M.,
RA Tanaka A., Tamiaki H.;
RT "Specific gene bciD for C7-methyl oxidation in bacteriochlorophyll e
RT biosynthesis of brown-colored green sulfur bacteria.";
RL PLoS ONE 8:E60026-E60026(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1677 / 4930 {ECO:0000312|EMBL:AOS84617.1,
RC ECO:0000312|Proteomes:UP000095185};
RA Liu Z., Tank M., Bryant D.A.;
RT "Genome sequence of Chlorobaculum limnaeum.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=RK-j-1;
RX PubMed=24496988; DOI=10.1007/s11120-014-9977-8;
RA Mizoguchi T., Harada J., Tsukatani Y., Tamiaki H.;
RT "Isolation and characterization of a new bacteriochlorophyll-c bearing a
RT neopentyl substituent at the 8-position from the bciD-deletion mutant of
RT the brown-colored green sulfur bacterium Chlorobaculum limnaeum.";
RL Photosyn. Res. 121:3-12(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DISRUPTION PHENOTYPE, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=DSM 1677 / 4930;
RX PubMed=27994052; DOI=10.1074/jbc.m116.767665;
RA Thweatt J.L., Ferlez B.H., Golbeck J.H., Bryant D.A.;
RT "BciD is a radical S-adenosyl-L-methionine (SAM) enzyme that completes
RT bacteriochlorophyllide e biosynthesis by oxidizing a methyl group into a
RT formyl group at C-7.";
RL J. Biol. Chem. 292:1361-1373(2017).
CC -!- FUNCTION: Involved in the biosynthesis of bacteriochlorophyll e (BChl
CC e). Catalyzes two consecutive hydroxylation reactions of the C-7 methyl
CC group of bacteriochlorophyllide c (BChlide c) to form a geminal diol
CC intermediate that spontaneously dehydrates to produce the formyl group
CC of bacteriochlorophyllide e (BChlide e) (PubMed:23560066,
CC PubMed:27994052). Also able to catalyze the same reaction for
CC bacteriochlorophyllide d (BChlide d) to give rise to
CC bacteriochlorophyllide f (BChlide f) (PubMed:27994052).
CC {ECO:0000269|PubMed:23560066, ECO:0000269|PubMed:27994052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a bacteriochlorophyllide c + H2O + 2 S-adenosyl-L-methionine =
CC 2 5'-deoxyadenosine + a bacteriochlorophyllide e + 2 H(+) + 2 L-
CC methionine; Xref=Rhea:RHEA:52252, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:90965, ChEBI:CHEBI:136512;
CC EC=1.17.98.2; Evidence={ECO:0000269|PubMed:27994052};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a bacteriochlorophyllide d + H2O + 2 S-adenosyl-L-methionine =
CC 2 5'-deoxyadenosine + a bacteriochlorophyllide f + 2 H(+) + 2 L-
CC methionine; Xref=Rhea:RHEA:55812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:90955, ChEBI:CHEBI:139237;
CC EC=1.17.98.2; Evidence={ECO:0000269|PubMed:27994052};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:27994052};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:27994052};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis. {ECO:0000305|PubMed:23560066}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC bacteriochlorophyll e (BChl e), accumulate bacteriochlorophyll c (BChl
CC c) and are green in color instead of the characteristic brownish color
CC (PubMed:23560066, PubMed:27994052). The mutant also has a novel homolog
CC containing a triple 8-methylated neopentyl substituent at the 8-
CC position (PubMed:24496988). {ECO:0000269|PubMed:23560066,
CC ECO:0000269|PubMed:24496988, ECO:0000269|PubMed:27994052}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
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DR EMBL; CP017305; AOS84617.1; -; Genomic_DNA.
DR EMBL; AB762294; BAN14903.1; -; Genomic_DNA.
DR RefSeq; WP_069810809.1; NZ_CP017305.1.
DR AlphaFoldDB; N0DKX5; -.
DR STRING; 274537.BIU88_11010; -.
DR EnsemblBacteria; AOS84617; AOS84617; BIU88_11010.
DR KEGG; clz:BIU88_11010; -.
DR OrthoDB; 325000at2; -.
DR BioCyc; MetaCyc:MON-19714; -.
DR BRENDA; 1.17.98.2; 10376.
DR UniPathway; UPA00669; -.
DR Proteomes; UP000095185; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster 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; 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; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR007197; rSAM.
DR SMART; SM00729; Elp3; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Photosynthesis;
KW S-adenosyl-L-methionine.
FT CHAIN 1..402
FT /note="Bacteriochlorophyllide c C-7(1)-hydroxylase"
FT /id="PRO_0000443059"
FT DOMAIN 104..359
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 120
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 132
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
SQ SEQUENCE 402 AA; 45115 MW; 16619EAD44F69569 CRC64;
MSTKRVITKE DIHLKARLLS EGAKVTVNKP PASGFNPFRA MVLNGSDLAT LVRQEPYTRL
EVQVNGDDVE FYDCGQHLAS GRMQEAFSWR SGKLSNGRPV DAAVIGMNQD IINIHYSYSC
DNNNTGRSCR FCFFFADQHI GVGKELAKMP FSKIEELAKE QAEAVKIATD AGWRGTLVII
GGLVDPSRRA QVADLVELVM APLREQVSPE VLNELHITAN LYPPDDFKEM EKWKASGLNS
TEFDLEVTHP DYFKAICPGK SATYPLEYWL EAQEASVKIF GPGRGTTSFI LMGLEPMNIM
LEGVEERMSK GVYPNMLVYQ PVPGADMFRM PPPNADWLVE ASEKVADLYI KYQDRFDMPL
AKDHRPGYTR MGRSQYIILA GDMLAYKLQE QGYELPEAYP VC
