CHLB_THEVB
ID CHLB_THEVB Reviewed; 508 AA.
AC Q8DGC6;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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}; OrderedLocusNames=tll2392;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(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 -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00353}.
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DR EMBL; BA000039; BAC09944.1; -; Genomic_DNA.
DR RefSeq; NP_683182.1; NC_004113.1.
DR RefSeq; WP_011058224.1; NC_004113.1.
DR PDB; 2XDQ; X-ray; 2.40 A; B=1-508.
DR PDBsum; 2XDQ; -.
DR AlphaFoldDB; Q8DGC6; -.
DR SMR; Q8DGC6; -.
DR STRING; 197221.22296120; -.
DR EnsemblBacteria; BAC09944; BAC09944; BAC09944.
DR KEGG; tel:tll2392; -.
DR PATRIC; fig|197221.4.peg.2512; -.
DR eggNOG; COG2710; Bacteria.
DR OMA; TTFQARD; -.
DR OrthoDB; 363662at2; -.
DR UniPathway; UPA00670; -.
DR EvolutionaryTrace; Q8DGC6; -.
DR Proteomes; UP000000440; Chromosome.
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 3D-structure; 4Fe-4S; ATP-binding; Chlorophyll biosynthesis; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..508
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_0000219805"
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"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2XDQ"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2XDQ"
FT TURN 62..67
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2XDQ"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 131..153
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 178..192
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:2XDQ"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 249..264
FT /evidence="ECO:0007829|PDB:2XDQ"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:2XDQ"
FT TURN 297..300
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 309..323
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 338..345
FT /evidence="ECO:0007829|PDB:2XDQ"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 358..368
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 377..386
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:2XDQ"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:2XDQ"
FT HELIX 411..438
FT /evidence="ECO:0007829|PDB:2XDQ"
SQ SEQUENCE 508 AA; 56317 MW; 90C9BFCF89DD0789 CRC64;
MKLAYWMYAG PAHIGTLRIA SSFKNVHGIM HAPLGDDYFN VMRSMLERER DFTPVTASIV
DRHVLARGSQ EKVVDNIIRK DTEEHPDLIV LTPTCTSSIL QEDLQNFVRR ASLSTTADVL
LADVNHYRVN ELQAADRTLE QIVQFYIDKA RRQGTLGTSK TPTPSVNIIG ITTLGFHNQH
DCRELKQLMA DLGIQVNLVI PAAATVHDLQ RLPQAWFNLV PYREIGGLTA QYLEREFGQP
SVRITPMGVV ETARCIRAIQ GVLNAQGAGV NYEAFIEQQT REVSQAAWFS RSIDCQNLTG
KKAVVFGDNT HAAAMTKILS REMGIHVVWA GTYCKYDADW FRAEVAGFCD EVLITDDHTV
VGDAIARVEP AAIFGTQMER HVGKRLNIPC GVIAAPIHIQ DFPVGYRPFL GYEGTNQLVD
LIYNSFTLGM EDHLLEIFGG HDTKAVIHKG LSADSDLTWT AAGLAELNKI PGFVRGKVKR
NTEKFAREQG ISEITVEVLY AAKEAVGA
