BCHB_RUBGI
ID BCHB_RUBGI Reviewed; 543 AA.
AC Q9JPA3; I0HUJ9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=RGE_33470;
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX NCBI_TaxID=983917;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=11343129; DOI=10.1007/s002390010163;
RA Igarashi N., Harada J., Nagashima S., Matsuura K., Shimada K.,
RA Nagashima K.V.P.;
RT "Horizontal transfer of the photosynthesis gene cluster and operon
RT rearrangement in purple bacteria.";
RL J. Mol. Evol. 52:333-341(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=22689232; DOI=10.1128/jb.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-Isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(2012).
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; AB034704; BAA94058.1; -; Genomic_DNA.
DR EMBL; AP012320; BAL96686.1; -; Genomic_DNA.
DR PIR; T50905; T50905.
DR RefSeq; WP_014429547.1; NC_017075.1.
DR AlphaFoldDB; Q9JPA3; -.
DR SMR; Q9JPA3; -.
DR STRING; 983917.RGE_33470; -.
DR EnsemblBacteria; BAL96686; BAL96686; RGE_33470.
DR KEGG; rge:RGE_33470; -.
DR PATRIC; fig|983917.3.peg.3272; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025470_0_0_4; -.
DR OMA; TTFQARD; -.
DR OrthoDB; 363662at2; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000007883; 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; Reference proteome.
FT CHAIN 1..543
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_0000219801"
FT ACT_SITE 287
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 422..423
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00353"
SQ SEQUENCE 543 AA; 58698 MW; 76ADF68BA2C1D067 CRC64;
MQLTLWTYEG PPHVGAMRVA TALDDVHYVL HAPQGDTYAD LLFTMIERLP RRPPVTYTTF
QARDLGGDTA ELFKTACSQA FERFRPNAML VGASCTAELI QDDPGGLARA LALPIPVVPL
ELPSYQRKEN WGASETFYQV VRTLAGPRAP APGTPRPARE PGAKPCCNLL GPTALGFRHR
DDVREITGLL NELGIEVRTV APLGASADDI ARLGEADFNV VLYPETAQQA AGWLQRFFGQ
PFTKTIPIGV KATKAFIAEV LQLAGLPADT PLPDALSRSP WYSRSVDSTY LTGKRVFIFG
DATHAIAAAR VATEEMGFTV VGLGTYSREF ARDVRDAAKH YGVEALITDD YLEVEAKVAE
LHPELVLGTQ MERHIAKRLG VPCAVISAPV HVQDFPARYS PQMGFEGANV LFDSWVHPLM
MGLEEHLLTM FRGDFEFHDG AAASHLGRAA VPPPAAAPAP AAESSDVPAV AETATAAATV
AAPAASAPIT VAQWAPDAQK ELQKIPFFVR GKARRNTERF AAERGLATIT VETLYDAKAH
FGR
