CHLB_LEPBY
ID CHLB_LEPBY Reviewed; 508 AA.
AC P95463;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 Leptolyngbya boryana (Plectonema boryanum).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Leptolyngbyaceae; Leptolyngbya.
OX NCBI_TaxID=1184;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP SUBUNIT.
RC STRAIN=ATCC 27894 / CCAP 1463/1 / IAM M-101 / PCC 6306 / UTEX 581;
RX PubMed=8673341; DOI=10.1093/oxfordjournals.pcp.a028948;
RA Fujita Y., Takagi H., Hase T.;
RT "Identification of the chlB gene and the gene product essential for the
RT light-independent chlorophyll biosynthesis in the cyanobacterium Plectonema
RT boryanum.";
RL Plant Cell Physiol. 37:313-323(1996).
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 ECO:0000269|PubMed:8673341}.
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 (Probable). {ECO:0000305|PubMed:8673341}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gere are unable to synthesize
CC chlorophyll, accumulating protochlorophyllide in darkness while
CC synthesizing chlorophyll normally in the light.
CC {ECO:0000269|PubMed:8673341}.
CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00353}.
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DR EMBL; D78208; BAA11312.1; -; Genomic_DNA.
DR AlphaFoldDB; P95463; -.
DR SMR; P95463; -.
DR BioCyc; MetaCyc:MON-19729; -.
DR UniPathway; UPA00670; -.
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 1: Evidence at protein level;
KW 4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Oxidoreductase; Photosynthesis.
FT CHAIN 1..508
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_0000219804"
FT ACT_SITE 294
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 429..430
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
SQ SEQUENCE 508 AA; 56820 MW; E607EA75D9B4EF94 CRC64;
MKLAYWMYAG PAHIGTLRIA SSFKNVHAIM HAPLGDDYFN VMRSMLERER DYTPVTTSVV
DRHVLARGSQ EKVVDNITRK DAEEHPDLIV LTPTCTSSIL QEDLQNFVER AQLEAKGDVM
LADVNHYRVN ELQAADRTLQ QIVQFYIAKA RKQGNLVTEK TEKPSVNIFG MTTLGFHNNH
DATELKKLMS DLGIEVNAIV PAGASVHELK SLPRAWFNLV PYRETGLLAA EFLQQEFNMP
YVDITPIGIV ETARCIRKIQ QVINAQGANV DYEPFIDQQT RFVSQAAWFS RSIDCQNLTG
KKAVVFGDNT HAAALTKILA REMGIHVLLA GTYCKYDEAW FREQVSEYCD DVLVSDDNGQ
IADAIARLEP AAIFGTQMER HVGKRLDIPC GVIAAPIHIQ NFPVGYKPFV GYEGSNQIVD
LIYNSFTLGM EDHLLEIFGG HDTKEVITKS VSADSDLNWS KDGLAELNRI PGFVRGKVKR
NTEKFARDRN ITQITAEVLY AAKEAVGA
