P26164 (BCHN_RHOCB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Light-independent protochlorophyllide reductase subunit N
Short name=DPOR subunit N
Short name=LI-POR subunit N
EC=1.18.-.-

Gene names

Name:	bchN
Ordered Locus Names:	RCAP_rcc00665

Organism

Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) [Complete proteome] [HAMAP]

Taxonomic identifier

272942 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter › Rhodobacter capsulatus

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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. HAMAP-Rule MF_00352
Pathway	Porphyrin biosynthesis; bacteriochlorophyll biosynthesis (light-independent). HAMAP-Rule MF_00352
Subunit structure	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.
Sequence similarities	Belongs to the BchN/ChlN family.

Ontologies

Keywords
Biological process	Bacteriochlorophyll biosynthesis Chlorophyll biosynthesis Photosynthesis
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	light-independent bacteriochlorophyll biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway photosynthesis, dark reaction Inferred from electronic annotation. Source: InterPro
Molecular_function	oxidoreductase activity, acting on iron-sulfur proteins as donors Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 424

424

Light-independent protochlorophyllide reductase subunit N HAMAP-Rule MF_00352

PRO_0000208596

Secondary structure

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424

Helix Strand Turn

Details...

Beta strand

11 – 13

3

Beta strand

15 – 18

4

Helix

27 – 30

4

Helix

31 – 37

7

Beta strand

41 – 47

7

Helix

49 – 59

11

Helix

60 – 64

5

Beta strand

68 – 73

6

Helix

76 – 79

4

Beta strand

80 – 82

3

Helix

85 – 98

14

Beta strand

105 – 110

6

Helix

112 – 116

5

Helix

121 – 131

11

Turn

133 – 135

3

Beta strand

137 – 142

6

Turn

145 – 147

3

Helix

152 – 161

10

Helix

162 – 164

3

Beta strand

173 – 177

5

Helix

181 – 193

13

Beta strand

199 – 203

5

Helix

207 – 209

3

Beta strand

218 – 223

6

Helix

227 – 235

9

Beta strand

239 – 241

3

Helix

248 – 262

15

Helix

267 – 286

20

Helix

289 – 292

4

Beta strand

296 – 299

4

Beta strand

301 – 304

4

Helix

306 – 315

10

Beta strand

320 – 327

8

Helix

331 – 338

8

Beta strand

346 – 350

5

Helix

353 – 363

11

Beta strand

366 – 370

5

Helix

372 – 379

8

Turn

380 – 382

3

Beta strand

385 – 387

3

Helix

388 – 391

4

Beta strand

397 – 399

3

Helix

402 – 420

19

Sequences

	Sequence		Length	Mass (Da)
	P26164 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: C90C75233802834D	FASTA	424	45,830
	10 20 30 40 50 60 MSLDSPTFGC TDSPVRRERG QKAVFCGLTS IVWLHRKMQD AFFLVVGSRT CAHLLQAAAG 70 80 90 100 110 120 VMIFAEPRFG TAVLEEQDLA GLADAHKELD REVAKLLERR PDIRQLFLVG SCPSEVLKLD 130 140 150 160 170 180 LDRAAERLSG LHAPHVRVYS YTGSGLDTTF TQGEDTCLAA MVPTLDTTEA AELIVVGALP 190 200 210 220 230 240 DVVEDQCLSL LTQLGVGPVR MLPARRSDIE PAVGPNTRFI LAQPFLGETT GALERRGAKR 250 260 270 280 290 300 IAAPFPFGEE GTTLWLKAVA DAYGVSAEKF EAVTAAPRAR AKKAIAAHLE TLTGKSLFMF 310 320 330 340 350 360 PDSQLEIPLA RFLARECGMK TTEIATPFLH KAIMAPDLAL LPSNTALTEG QDLEAQLDRH 370 380 390 400 410 420 EAINPDLTVC GLGLANPLEA KGHATKWAIE LVFTPVHFYE QAGDLAGLFS RPLRRRALLN GGAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus and identification of the third subunit of light-independent protochlorophyllide reductase in bacteria and plants." Burke D.H., Alberti M., Hearst J.E. J. Bacteriol. 175:2414-2422(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[2]	"Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003." Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R. J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[3]	"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." Fujita Y., Bauer C.E. J. Biol. Chem. 275:23583-23588(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: SB1003 / CB1029.
[4]	Fujita Y. Unpublished observations (JUL-2001) Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z11165 Genomic DNA. Translation: CAA77526.1.
CP001312 Genomic DNA. Translation: ADE84430.1.

PIR

B49851.

RefSeq

YP_003576837.1. NC_014034.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3AEK	X-ray	2.30	A/C	2-424	[»]
3AEQ	X-ray	2.90	A/C	2-424	[»]
3AER	X-ray	2.80	A/C	2-424	[»]
3AES	X-ray	2.50	A/C	2-424	[»]
3AET	X-ray	2.91	A/C	2-424	[»]
3AEU	X-ray	2.90	A/C	2-424	[»]

ProteinModelPortal

P26164.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59277N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

ADE84430; ADE84430; RCAP_rcc00665.

GeneID

9003494.

KEGG

rcp:RCAP_rcc00665.

PATRIC

35501398. VBIRhoCap134200_0676.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HOG000265994.

KO

K04038.

OMA

MIFAEPR.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13269.
RCAP272942:GJIY-678-MONOMER.

UniPathway

UPA00671.

Family and domain databases

HAMAP

MF_00352. ChlN_BchN.

InterPro

IPR000510. Nase/OxRdtase_comp1.
IPR005970. Protochl_reductN.
[Graphical view]

Pfam

PF00148. Oxidored_nitro. 1 hit.
[Graphical view]

PIRSF

PIRSF000162. P_chlorophyll_rd. 1 hit.

TIGRFAMs

TIGR01279. DPOR_bchN. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P26164.

Entry information

Entry name

BCHN_RHOCB

Accession

Primary (citable) accession number: P26164
Secondary accession number(s): D5ANS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program