BCHB_CHLL3
ID BCHB_CHLL3 Reviewed; 525 AA.
AC Q3B6C7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=bchB {ECO:0000255|HAMAP-Rule:MF_00353}; OrderedLocusNames=Plut_0216;
OS Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS luteolum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=319225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 273 / BCRC 81028 / 2530;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelodictyon luteolum DSM 273.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (BchN-BchB) 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; bacteriochlorophyll
CC biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_00353}.
CC -!- SUBUNIT: Protochlorophyllide reductase is composed of three subunits;
CC BchL, BchN and BchB. Forms a heterotetramer of two BchB and two BchN
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; CP000096; ABB23104.1; -; Genomic_DNA.
DR RefSeq; WP_011356979.1; NC_007512.1.
DR AlphaFoldDB; Q3B6C7; -.
DR SMR; Q3B6C7; -.
DR STRING; 319225.Plut_0216; -.
DR EnsemblBacteria; ABB23104; ABB23104; Plut_0216.
DR KEGG; plt:Plut_0216; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025470_0_0_10; -.
DR OMA; TTFQARD; -.
DR OrthoDB; 363662at2; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000002709; 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:0036070; P:light-independent bacteriochlorophyll 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 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis;
KW Chlorophyll biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Oxidoreductase; Photosynthesis.
FT CHAIN 1..525
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_1000048405"
FT REGION 447..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 292
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 428..429
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
SQ SEQUENCE 525 AA; 57411 MW; 167F301D499224CF CRC64;
MRLAFWLYEG TALHGISRVT NSMKGVHTVY HAPQGDDYIT ATYTMLERTP EFPALSISVV
RGRDLAQGVS RLPATLQQVE EHYHPELSVI APSCSTALLQ EDLHQLAAQS GVPQDKLMVY
AVNPFRVTEN EAADGLLTAL VKRYAAEGPK TAAPTVNLLG FTSLGFHLKA NLTSIRRLLT
TLGVKVNVVA PWGAGIADLK RLPEAWLTIA PFREIGQTAA AYLEETFGVP TEYGTPLGVE
PTLRWLRAVI EKLNTVGAKE GATPIAMPEL HAFSLDGMSA PSGVPWFART ADMESFSNKK
AFVFGDATTT VAMVKFLRDE LGMQIIGAGT YLERHADWVR KELDGYLPGA LMVTERFQDV
AQVIEDEMPD LVCGTQMERH SCRKLDVPCM VVCPPTHIEN HLLGYYPFLG FDGADVIADR
VYISCKLGLE KHLIDFFGDA GLEYEEPSAS SENGSAPLSA GTATPAAAPE EGGMAWTDEA
ETMLKKVPFF VRKKVRKNTE NFAEENGESR VSVEVFRRAK ESLGG
