[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 23782 / LMG 2373 / NCIB 11773 / SB1003 / St. Louis; PubMed=8385667 [NCBI, ExPASy, EBI, Israel, Japan] 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]	PROTEIN SEQUENCE OF 1-6, AND CHARACTERIZATION. STRAIN=SB1003 / CB1029; DOI=10.1074/jbc.M002904200; PubMed=10811655 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[3]	CHARACTERIZATION. Fujita Y.; Unpublished observations (JUL-2001).

Comments

FUNCTION: Uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). The bchN-bchB pair binds Pchlide. This reaction is light-independent.
PATHWAY: Porphyrin biosynthesis; bacteriochlorophyll biosynthesis (light-independent).
SUBUNIT: Protochlorophyllide reductase is thought to be composed of three subunits; bchL, bchN and bchB. Could form a heterotetramer of two bchB and two bchN subunits.
SIMILARITY: Belongs to the chlB/bchB/bchZ family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z11165; CAA77525.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C49851; C49851.

3D structure databases

ModBase

P26163.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13270; -.

Ontologies

GO:0016730;	Molecular function: oxidoreductase activity, acting on iron-sulfur proteins as donors (inferred from electronic annotation from HAMAP).
GO:0030494;	Biological process: bacteriochlorophyll biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019685;	Biological process: photosynthesis, dark reaction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00353; -; 1.
PBIL [Tree]

InterPro

IPR000510; Nase/OxRdtase_comp1.
IPR013580; PCP_red.
IPR005969; Protochl_reductB.
IPR016209; Protochlorophyllide_Rdtase.
Graphical view of domain structure.

Pfam

PF00148; Oxidored_nitro; 1.
PF08369; PCP_red; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000163; PCP_ChlB; 1.

TIGRFAMs

TIGR01278; DPOR_BchB; 1.

Other

ProtoNet

P26163.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; Direct protein sequencing; Oxidoreductase; Photosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 525`	`525`		`Light-independent protochlorophyllide reductase subunit B.`	`PRO_0000219800`

Sequence information

Length: 525 AA [This is the length of the unprocessed precursor]

Molecular weight: 57192 Da [This is the MW of the unprocessed precursor]

CRC64: 4322A6D9F535C3F5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLTLWTYEG PPHVGAMRVA TAMKDLQLVL HGPQGDTYAD LLFTMIERRN ARPPVSFSTF 

        70         80         90        100        110        120 
EASHMGTDTA ILLKDALAAA HARYKPQAMA VALTCTAELL QDDPNGISRA LNLPVPVVPL 

       130        140        150        160        170        180 
ELPSYSRKEN YGADETFRAL VRALAVPMER TPEVTCNLLG ATALGFRHRD DVAEVTKLLA 

       190        200        210        220        230        240 
TMGIKVNVCA PLGASPDDLR KLGQAHFNVL MYPETGESAA RHLERACKQP FTKIVPIGVG 

       250        260        270        280        290        300 
ATRDFLAEVS KITGLPVVTD ESTLRQPWWS ASVDSTYLTG KRVFIFGDGT HVIAAARIAA 

       310        320        330        340        350        360 
KEVGFEVVGM GCYNREMARP LRTAAAEYGL EALITDDYLE VEKAIEAAAP ELILGTQMER 

       370        380        390        400        410        420 
NIAKKLGLPC AVISAPVHVQ DFPARYAPQM GFEGANVLFD TWVHPLVMGL EEHLLTMFRE 

       430        440        450        460        470        480 
DFEFHDAAGA SHHGGKAVAR EESPVAPADL APAATSDTPA APSPVVVTQA SGEIRWMPEA 

       490        500        510        520 
ERELRKIPFF VRGKAKRNTE LYAAHKGVCD ITVETLYEAK AHYAR

P26163 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools