CHLB_ANTAG
ID CHLB_ANTAG Reviewed; 513 AA.
AC Q85AC2;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
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 Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
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 -!- RNA EDITING: Modified_positions=31 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 33 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 54 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 91 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 93 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 100 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 104 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 121 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 127 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 128 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 133 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 135 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 137 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 141 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 172 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 219 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 246 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 257 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 283 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 284 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 291 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 378 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 401 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 407 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 472 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions
CC 128, 133, 137, 141, 257, 283 and 284 are modified to sense codons.;
CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00353}.
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DR EMBL; AB086179; BAC55338.1; -; Genomic_DNA.
DR EMBL; AB087430; BAC55429.1; -; mRNA.
DR RefSeq; NP_777402.1; NC_004543.1.
DR AlphaFoldDB; Q85AC2; -.
DR SMR; Q85AC2; -.
DR GeneID; 2553487; -.
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; 1.
DR Pfam; PF08369; PCP_red; 1.
DR PIRSF; PIRSF000163; PCP_ChlB; 1.
DR TIGRFAMs; TIGR01278; DPOR_BchB; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Chloroplast; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis; Plastid; RNA editing.
FT CHAIN 1..513
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_0000219809"
FT ACT_SITE 299
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 434..435
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
SQ SEQUENCE 513 AA; 58191 MW; D77350BAB143E8A6 CRC64;
MKLAYWMYAG PAHIGTLRVA SSFKNVHAIM HAPLGDDYFN VMRSMLERER DFTPVTASIV
DRHVLARGSQ EKVVDNIMRK DKEECPDLIV LTPTCTSSIL QEDLQNFVDR ASISVNSDVI
LADVNHYRVN ELQAADRTLE QIVRYYLDKA RRQGKLNQSI TDVPSANIIG IFTLGFHNQH
DCRELKRLLK DLGIKINQVI PEGGFVEDLE KLPKAWFNLI PYREVGLMTA IYLEKEFGMP
YVSITPMGIA DIVQCIRQIQ KRVNTWTHFL LNQKLDYELY IDQQTRFISQ AAWFSRSIDC
QNLTGKKAVV FGDATHASSM TKILAQEMGI RVSCAGTYCK HDAEWFEEQV QGFCDEILIT
DDHTQVGDTI ARIEPSAIFG TQMERHIGKR LDIPCGVISS PVHIQNFPLG YRPFLGYEGT
NQIADLVYNS FTLGMEDHLL EIFGGHDTKE VITKSLSTDN DLTWNSESQL ELNKIPGFVR
GKIKRNTERF ARQNGITGIT VEVMYAAKEA LNA
