BCHB_CHLPD
ID BCHB_CHLPD Reviewed; 535 AA.
AC A1BIZ8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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};
GN OrderedLocusNames=Cpha266_2387;
OS Chlorobium phaeobacteroides (strain DSM 266).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000492; ABL66375.1; -; Genomic_DNA.
DR RefSeq; WP_011746158.1; NC_008639.1.
DR AlphaFoldDB; A1BIZ8; -.
DR SMR; A1BIZ8; -.
DR STRING; 290317.Cpha266_2387; -.
DR EnsemblBacteria; ABL66375; ABL66375; Cpha266_2387.
DR KEGG; cph:Cpha266_2387; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025470_0_0_10; -.
DR OMA; TTFQARD; -.
DR OrthoDB; 363662at2; -.
DR UniPathway; UPA00671; -.
DR Proteomes; UP000008701; 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..535
FT /note="Light-independent protochlorophyllide reductase
FT subunit B"
FT /id="PRO_1000048401"
FT REGION 447..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Polar residues"
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 535 AA; 58733 MW; 3C49145586D44108 CRC64;
MRLAFWLYEG TALHGISRIT NSMKGVHTVY HAPQGDDYIT ATYTMLERTP DFPGLSISVV
RGRDLAQGVS RLPSTLQQVD HHYSPDLTVI APSCSTALLQ EDLNQLAAHS GVPSEKLLVY
ALNPFRVSEN EAADGLFTEL VKRYAVAQEK TPTPSVNLLG FTSLGFHLRA NLTSLRRMLE
ALGIAVNVVA PWGSGIDDLA KLPAAWLNIA PYREIGATAA AYLDETCGMP AMYEAPIGVE
PTTAWLRKLL DEINRIAGQK GLSRLAMPAP RAFSLDGLSA PSGVPWFART ADMESFSNKR
AFVFGDATHT VALVKFLRDE LGMQIIGAGT YLERHADWVR KELDGYLPGE LMVTDRFQDV
AKFIDDQMPD LVCGTQMERH SCRKLDVPCM VICPPTHIEN HLLGYYPFFG FDGADVIADR
VYLSCKLGLE KHLIDFFGDA GLEYEESDDA AKAEPDQPVS NAHGHTESKT VSQGEPIASD
EGGISWSDEA ETMLKKVPFF VRKKVRKNTE DFALGIGESC VTAEVFRKAK ESLGG
