CHLB_CHLRE
ID CHLB_CHLRE Reviewed; 687 AA.
AC P36437; B7U1E6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Light-independent protochlorophyllide reductase subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE Short=DPOR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE Short=LI-POR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
DE EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00353};
GN Name=chlB {ECO:0000255|HAMAP-Rule:MF_00353};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=137c / CC-125;
RX PubMed=8219066; DOI=10.1007/bf00029006;
RA Liu X.-Q., Xu H., Huang C.;
RT "Chloroplast chlB gene is required for light-independent chlorophyll
RT accumulation in Chlamydomonas reinhardtii.";
RL Plant Mol. Biol. 23:297-308(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=21gr / CC-1690;
RX PubMed=8305874; DOI=10.2307/3869697;
RA Li J., Goldschmidt-Clermont M., Timko M.P.;
RT "Chloroplast-encoded chlB is required for light-independent
RT protochlorophyllide reductase activity in Chlamydomonas reinhardtii.";
RL Plant Cell 5:1817-1829(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [4]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
CC -!- FUNCTION: Component of the dark-operative protochlorophyllide reductase
CC (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of
CC protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This
CC reaction is light-independent. The NB-protein (ChlN-ChlB) is the
CC catalytic component of the complex. {ECO:0000255|HAMAP-Rule:MF_00353}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2
CC phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-
CC 4S]-[ferredoxin]; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002,
CC Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33722, ChEBI:CHEBI:33723, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83348, ChEBI:CHEBI:83350, ChEBI:CHEBI:456216; EC=1.3.7.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00353};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00353};
CC Note=Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at
CC the heterodimer interface by residues from both subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00353};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00353}.
CC -!- SUBUNIT: Protochlorophyllide reductase is composed of three subunits;
CC ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00353}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00353}.
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DR EMBL; L13782; AAA16321.1; -; Genomic_DNA.
DR EMBL; U02526; AAB06265.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50093.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00906.1; -; Genomic_DNA.
DR PIR; S39491; S39491.
DR RefSeq; NP_958360.1; NC_005353.1.
DR AlphaFoldDB; P36437; -.
DR SMR; P36437; -.
DR STRING; 3055.DAA00906; -.
DR PaxDb; P36437; -.
DR PRIDE; P36437; -.
DR GeneID; 2716966; -.
DR KEGG; cre:ChreCp003; -.
DR eggNOG; ENOG502QUNZ; Eukaryota.
DR HOGENOM; CLU_025470_0_0_1; -.
DR InParanoid; P36437; -.
DR OrthoDB; 538441at2759; -.
DR BioCyc; MetaCyc:CHRECP003-MON; -.
DR UniPathway; UPA00670; -.
DR Proteomes; UP000006906; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
DR GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
DR Gene3D; 1.10.8.550; -; 1.
DR HAMAP; MF_00353; ChlB_BchB; 1.
DR InterPro; IPR013580; LI-POR_suB-like_C.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR042298; P-CP_red_C.
DR InterPro; IPR005969; Protochl_reductB.
DR Pfam; PF00148; Oxidored_nitro; 3.
DR Pfam; PF08369; PCP_red; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Chloroplast; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis; Plastid; Reference proteome.
FT CHAIN 1..687
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_0000219817"
FT ACT_SITE 441
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
FT BINDING 36
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
FT BINDING 576..577
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
FT CONFLICT 44
FT /note="S -> T (in Ref. 1; AAA16321)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="N -> D (in Ref. 1; AAA16321)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="R -> A (in Ref. 1; AAA16321)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="G -> V (in Ref. 1; AAA16321)"
FT /evidence="ECO:0000305"
FT CONFLICT 623..627
FT /note="SNVVS -> FKCSVF (in Ref. 1; AAA16321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 76625 MW; 7358517D85817882 CRC64;
MKLAYWMYAG PAHIGVLRVS SSFKNVHAIM HAPLGDDYFN VMRSMLERER DFTPVTASIV
DRHVLARGSQ EKVVENITRK NKEETPDLIL LTPTCTSSIL QEDLHNFVES ALAKPVQIDE
HADHKVTQQS ALSSVSPLLP LEENTLIVSE LDKKLSPSSK LHINMPNICI PEGEGEGEQT
KNSIFVKSAT LTNLSEEELL NQEHHTKTRN HSDVILADVN HYRVNELQAA DRTLEQIVRY
YISQAQKQNC LNITKTAKPS VNIIGIFTLG FHNQHDCREL KRLFNDLGIQ INEIIPEGGN
VHNLKKLPQA WFNFVPYREI GLMTAMYLKS EFNMPYVAIT PMGLIDTAAC IRSICKIITT
QLLNQTATVQ EPSKFIYPKA TSLEQTNILE TSQKETILKD NPDSGNTLST TVEEIETLFN
KYIDQQTRFV SQAAWFSRSI DCQNLTGKKA VVFGDATHSA AMTKLLAREM GIKVSCAGTY
CKHDADWFRE QVSGFCDQVL ITDDHTQVGD MIAQLEPAAI FGTQMERHVG KRLDIPCGVI
SAPVHIQNFP LGYRPFLGYE GTNQIADLVY NSFNLGMEDH LLQIFGGHDS ENNSSIATHL
NTNNAINLAP GYLPEGEGSS RTSNVVSTIS SEKKAIVWSP EGLAELNKVP GFVRGKVKRN
TEKYALQKNC SMITVEVMYA AKEALSA
