CHLB_OLTVI
ID CHLB_OLTVI Reviewed; 559 AA.
AC Q20EY2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 Oltmannsiellopsis viridis (Marine flagellate) (Oltmannsiella viridis).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; Oltmannsiellopsidales;
OC Oltmannsiellopsidaceae; Oltmannsiellopsis.
OX NCBI_TaxID=51324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16472375; DOI=10.1186/1741-7007-4-3;
RA Pombert J.-F., Lemieux C., Turmel M.;
RT "The complete chloroplast DNA sequence of the green alga Oltmannsiellopsis
RT viridis reveals a distinctive quadripartite architecture in the chloroplast
RT genome of early diverging ulvophytes.";
RL BMC Biol. 4:3-3(2006).
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; DQ291132; ABB81931.1; -; Genomic_DNA.
DR RefSeq; YP_635863.1; NC_008099.1.
DR AlphaFoldDB; Q20EY2; -.
DR SMR; Q20EY2; -.
DR GeneID; 4100110; -.
DR UniPathway; UPA00670; -.
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 InterPro; IPR016209; Protochlorophyllide_Rdtase.
DR Pfam; PF00148; Oxidored_nitro; 2.
DR Pfam; PF08369; PCP_red; 1.
DR PIRSF; PIRSF000163; PCP_ChlB; 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.
FT CHAIN 1..559
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_0000324050"
FT ACT_SITE 348
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 483..484
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
SQ SEQUENCE 559 AA; 63186 MW; 0BEF0FCD15F4CC4D CRC64;
MKLAYWMYSG PAHIGTLRVA SSFKNVHAIM HAPLGDDYFN VMRSMLQRER DFTPVTASIV
DRHVLARGSQ EKVVDNITRK DKEDNPDLIL LTPTCTSSIL QEDLQNFVNQ AELDLETDVI
LADVNHYRVN ELQAADRTLE QITRHYIEKA KRQGQLDIQK SEKPTANILG VFTLGFHNQH
DCRELKRLLN DLGIEVNEII PEGAFVESLK NLPKAWFNLI PYREVGLMTA QYLKKEFNMP
YISTTPMGIV DTATCVREIC KTVASLRLSF GVDTPQKQLK ETNISSTKVD LVLKVEENRE
AKPLNTSMEV LGESKLRFGP LTNFDVEKYI DQQTRFISQA AWFSRSVDCQ NLTGKKAIVF
GDATHAASMT KILTREMGLY VLCAGTYCKH DADWFREQVQ GFCDSVLITD DHTEIGNIIA
QYEPDCIFGT QMERHVGKRL DIPCGVISAP VHIQNFPLGY RPFLGYEGIN QIADLVYNSF
SLGMEEHLLE IFGGHDTKEV ISDSLSTETG LEWTSEGLTE LNKVPGFVRN KVKRNVEKFA
QQQNISKISA DVMYAAKEA