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Light-independent protochlorophyllide reductase subunit B (DPOR subunit B) (LI-POR subunit B) (EC 1.3.7.7)

 BCHB_RHOCB              Reviewed;         525 AA.
P26163; D5ANS5;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
28-FEB-2018, entry version 102.
RecName: Full=Light-independent protochlorophyllide reductase subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
Short=DPOR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
Short=LI-POR subunit B {ECO:0000255|HAMAP-Rule:MF_00353};
EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00353, ECO:0000269|PubMed:18358835};
Name=bchB {ECO:0000255|HAMAP-Rule:MF_00353}; Synonyms=bchK;
OrderedLocusNames=RCAP_rcc00664;
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Rhodobacter.
NCBI_TaxID=272942;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
PubMed=8385667; DOI=10.1128/jb.175.8.2414-2422.1993;
Burke D.H., Alberti M., Hearst J.E.;
"bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus
and identification of the third subunit of light-independent
protochlorophyllide reductase in bacteria and plants.";
J. Bacteriol. 175:2414-2422(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
PubMed=20418398; DOI=10.1128/JB.00366-10;
Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
Haselkorn R.;
"Complete genome sequence of the photosynthetic purple nonsulfur
bacterium Rhodobacter capsulatus SB 1003.";
J. Bacteriol. 192:3545-3546(2010).
[3]
PROTEIN SEQUENCE OF 1-6, AND CHARACTERIZATION.
STRAIN=SB1003 / CB1029;
PubMed=10811655; DOI=10.1074/jbc.M002904200;
Fujita Y., Bauer C.E.;
"Reconstitution of light-independent protochlorophyllide reductase
from purified bchL and bchN-bchB subunits. In vitro confirmation of
nitrogenase-like features of a bacteriochlorophyll biosynthesis
enzyme.";
J. Biol. Chem. 275:23583-23588(2000).
[4]
CHARACTERIZATION.
Fujita Y.;
Unpublished observations (JUL-2001).
[5]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18358835; DOI=10.1016/j.febslet.2008.03.018;
Nomata J., Ogawa T., Kitashima M., Inoue K., Fujita Y.;
"NB-protein (BchN-BchB) of dark-operative protochlorophyllide
reductase is the catalytic component containing oxygen-tolerant Fe-S
clusters.";
FEBS Lett. 582:1346-1350(2008).
[6]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH BCHN SUBUNIT;
SUBSTRATE AND 4FE-4S CLUSTER AND OF MUTANTS ALA-36 AND CYS-36,
FUNCTION, SUBUNIT, COFACTOR, REACTION MECHANISM, ACTIVE SITE, AND
MUTAGENESIS OF ASP-36; CYS-95; ASP-274; MET-408 AND LEU-410.
PubMed=20400946; DOI=10.1038/nature08950;
Muraki N., Nomata J., Ebata K., Mizoguchi T., Shiba T., Tamiaki H.,
Kurisu G., Fujita Y.;
"X-ray crystal structure of the light-independent protochlorophyllide
reductase.";
Nature 465:110-114(2010).
-!- FUNCTION: Component of the dark-operative protochlorophyllide
reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce
ring D of protochlorophyllide (Pchlide) to form chlorophyllide a
(Chlide). This reaction is light-independent. The NB-protein
(BchN-BchB) is the catalytic component of the complex.
{ECO:0000255|HAMAP-Rule:MF_00353, ECO:0000269|PubMed:18358835,
ECO:0000269|PubMed:20400946}.
-!- CATALYTIC ACTIVITY: Protochlorophyllide a + reduced ferredoxin + 2
ATP + 2 H(2)O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2
phosphate. {ECO:0000255|HAMAP-Rule:MF_00353,
ECO:0000269|PubMed:18358835}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000255|HAMAP-Rule:MF_00353,
ECO:0000269|PubMed:20400946};
Note=Binds 1 [4Fe-4S] cluster per heterodimer (PubMed:20400946).
The cluster is bound at the heterodimer interface by residues from
both subunits (PubMed:20400946). {ECO:0000255|HAMAP-Rule:MF_00353,
ECO:0000269|PubMed:20400946};
-!- PATHWAY: Porphyrin-containing compound metabolism;
bacteriochlorophyll biosynthesis (light-independent).
{ECO:0000255|HAMAP-Rule:MF_00353}.
-!- SUBUNIT: Protochlorophyllide reductase is composed of three
subunits; BchL, BchN and BchB. Forms a heterotetramer of two BchB
and two BchN subunits (PubMed:20400946). {ECO:0000255|HAMAP-
Rule:MF_00353, ECO:0000269|PubMed:20400946}.
-!- INTERACTION:
P26164:bchN; NbExp=3; IntAct=EBI-9017546, EBI-9017544;
-!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family.
{ECO:0000255|HAMAP-Rule:MF_00353}.
-----------------------------------------------------------------------
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EMBL; Z11165; CAA77525.1; -; Genomic_DNA.
EMBL; CP001312; ADE84429.1; -; Genomic_DNA.
PIR; C49851; C49851.
RefSeq; WP_013066408.1; NC_014034.1.
PDB; 3AEK; X-ray; 2.30 A; B/D=1-525.
PDB; 3AEQ; X-ray; 2.90 A; B/D=1-525.
PDB; 3AER; X-ray; 2.80 A; B/D=1-525.
PDB; 3AES; X-ray; 2.50 A; B/D=1-525.
PDB; 3AET; X-ray; 2.91 A; B/D=1-525.
PDB; 3AEU; X-ray; 2.90 A; B/D=1-525.
PDBsum; 3AEK; -.
PDBsum; 3AEQ; -.
PDBsum; 3AER; -.
PDBsum; 3AES; -.
PDBsum; 3AET; -.
PDBsum; 3AEU; -.
ProteinModelPortal; P26163; -.
SMR; P26163; -.
DIP; DIP-59276N; -.
IntAct; P26163; 1.
STRING; 272942.RCAP_rcc00664; -.
EnsemblBacteria; ADE84429; ADE84429; RCAP_rcc00664.
GeneID; 31489610; -.
KEGG; rcp:RCAP_rcc00664; -.
eggNOG; ENOG4105EVY; Bacteria.
eggNOG; COG2710; LUCA.
HOGENOM; HOG000032963; -.
KO; K04039; -.
OMA; IPCAVIS; -.
OrthoDB; POG091H1082; -.
BioCyc; MetaCyc:MONOMER-13270; -.
BioCyc; RCAP272942:G1GUE-668-MONOMER; -.
BRENDA; 1.3.7.7; 5381.
UniPathway; UPA00671; -.
EvolutionaryTrace; P26163; -.
Proteomes; UP000002361; Chromosome.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
GO; GO:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
HAMAP; MF_00353; ChlB_BchB; 1.
InterPro; IPR000510; Nase/OxRdtase_comp1.
InterPro; IPR013580; P-CP/CP_red_C.
InterPro; IPR005969; Protochl_reductB.
InterPro; IPR016209; Protochlorophyllide_Rdtase.
Pfam; PF00148; Oxidored_nitro; 1.
Pfam; PF08369; PCP_red; 1.
PIRSF; PIRSF000163; PCP_ChlB; 1.
TIGRFAMs; TIGR01278; DPOR_BchB; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; ATP-binding; Bacteriochlorophyll biosynthesis;
Chlorophyll biosynthesis; Complete proteome;
Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
Nucleotide-binding; Oxidoreductase; Photosynthesis;
Reference proteome.
CHAIN 1 525 Light-independent protochlorophyllide
reductase subunit B.
/FTId=PRO_0000219800.
REGION 409 410 Substrate binding.
{ECO:0000269|PubMed:20400946}.
ACT_SITE 274 274 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_00353,
ECO:0000269|PubMed:20400946}.
METAL 36 36 Iron-sulfur (4Fe-4S); shared with
heterodimeric partner.
{ECO:0000269|PubMed:20400946}.
MUTAGEN 36 36 D->A: Retains 13% activity.
{ECO:0000269|PubMed:20400946}.
MUTAGEN 36 36 D->C,S: Almost no enzymatic activity.
{ECO:0000269|PubMed:20400946}.
MUTAGEN 95 95 C->A: Does not form heterotetramers.
{ECO:0000269|PubMed:20400946}.
MUTAGEN 274 274 D->A: Almost no enzymatic activity.
{ECO:0000269|PubMed:20400946}.
MUTAGEN 408 408 M->A: Retains 85% activity.
{ECO:0000269|PubMed:20400946}.
MUTAGEN 410 410 L->A: Almost no enzymatic activity.
{ECO:0000269|PubMed:20400946}.
STRAND 2 5 {ECO:0000244|PDB:3AEK}.
HELIX 12 20 {ECO:0000244|PDB:3AEK}.
STRAND 23 31 {ECO:0000244|PDB:3AEK}.
HELIX 36 39 {ECO:0000244|PDB:3AEK}.
HELIX 40 45 {ECO:0000244|PDB:3AEK}.
STRAND 54 57 {ECO:0000244|PDB:3AEK}.
HELIX 62 64 {ECO:0000244|PDB:3AEK}.
HELIX 68 84 {ECO:0000244|PDB:3AEK}.
STRAND 87 93 {ECO:0000244|PDB:3AEK}.
HELIX 97 99 {ECO:0000244|PDB:3AEK}.
HELIX 104 111 {ECO:0000244|PDB:3AEK}.
STRAND 117 119 {ECO:0000244|PDB:3AEK}.
TURN 124 126 {ECO:0000244|PDB:3AEK}.
HELIX 129 144 {ECO:0000244|PDB:3AEK}.
STRAND 155 161 {ECO:0000244|PDB:3AEK}.
HELIX 168 180 {ECO:0000244|PDB:3AEK}.
TURN 181 183 {ECO:0000244|PDB:3AEK}.
STRAND 185 191 {ECO:0000244|PDB:3AEK}.
HELIX 196 200 {ECO:0000244|PDB:3AEK}.
HELIX 201 204 {ECO:0000244|PDB:3AEK}.
STRAND 205 210 {ECO:0000244|PDB:3AEK}.
HELIX 213 226 {ECO:0000244|PDB:3AEK}.
HELIX 239 253 {ECO:0000244|PDB:3AEK}.
HELIX 266 271 {ECO:0000244|PDB:3AEK}.
HELIX 273 278 {ECO:0000244|PDB:3AEK}.
STRAND 282 285 {ECO:0000244|PDB:3AEK}.
HELIX 289 301 {ECO:0000244|PDB:3AEK}.
STRAND 306 313 {ECO:0000244|PDB:3AEK}.
HELIX 315 317 {ECO:0000244|PDB:3AEK}.
HELIX 318 327 {ECO:0000244|PDB:3AEK}.
HELIX 338 348 {ECO:0000244|PDB:3AEK}.
STRAND 351 355 {ECO:0000244|PDB:3AEK}.
HELIX 357 366 {ECO:0000244|PDB:3AEK}.
STRAND 370 372 {ECO:0000244|PDB:3AEK}.
STRAND 374 376 {ECO:0000244|PDB:3AEK}.
HELIX 379 381 {ECO:0000244|PDB:3AEK}.
HELIX 391 403 {ECO:0000244|PDB:3AEK}.
HELIX 409 417 {ECO:0000244|PDB:3AEK}.
SEQUENCE 525 AA; 57192 MW; 4322A6D9F535C3F5 CRC64;
MKLTLWTYEG PPHVGAMRVA TAMKDLQLVL HGPQGDTYAD LLFTMIERRN ARPPVSFSTF
EASHMGTDTA ILLKDALAAA HARYKPQAMA VALTCTAELL QDDPNGISRA LNLPVPVVPL
ELPSYSRKEN YGADETFRAL VRALAVPMER TPEVTCNLLG ATALGFRHRD DVAEVTKLLA
TMGIKVNVCA PLGASPDDLR KLGQAHFNVL MYPETGESAA RHLERACKQP FTKIVPIGVG
ATRDFLAEVS KITGLPVVTD ESTLRQPWWS ASVDSTYLTG KRVFIFGDGT HVIAAARIAA
KEVGFEVVGM GCYNREMARP LRTAAAEYGL EALITDDYLE VEKAIEAAAP ELILGTQMER
NIAKKLGLPC AVISAPVHVQ DFPARYAPQM GFEGANVLFD TWVHPLVMGL EEHLLTMFRE
DFEFHDAAGA SHHGGKAVAR EESPVAPADL APAATSDTPA APSPVVVTQA SGEIRWMPEA
ERELRKIPFF VRGKAKRNTE LYAAHKGVCD ITVETLYEAK AHYAR


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