Reviewed, UniProtKB/Swiss-Prot O05783 (FPRA_MYCTU)

Names and origin

Protein names

Recommended name:
    NADPH-ferredoxin reductase fprA
      Short name=NFR
    EC=1.18.1.2

Gene names

Name:	fprA
Ordered Locus Names:	Rv3106, MT3189
ORF Names:	MTCY164.16

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May serve as electron transfer protein and supply electrons to P450 systems.
Catalytic activity	2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.
Cofactor	FAD.
Subunit structure	Monomer. Ref.5 Ref.6
Sequence similarities	Belongs to the ferredoxin--NADP reductase type 1 family.

Ontologies

Keywords
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro ferredoxin-NADP+ reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 456

456

NADPH-ferredoxin reductase fprA

PRO_0000087329

Regions

Nucleotide binding

155 – 158

4

NADP

Nucleotide binding

199 – 200

2

NADP

Nucleotide binding

366 – 368

3

FAD

Sites

Binding site

14

1

FAD; via amide nitrogen

Binding site

40

1

FAD

Binding site

48

1

FAD; via amide nitrogen

Binding site

84

1

FAD; via amide nitrogen and carbonyl oxygen

Binding site

110

1

NADP

Binding site

211

1

NADP

Binding site

359

1

FAD; via amide nitrogen

Binding site

366

1

NADP; via amide nitrogen

Experimental info

Mutagenesis

57

1

H → A or Q: Reduces activity 4-fold.

Mutagenesis

214

1

E → A: No effect on activity. Decreases Km for NADP 2-fold.

Secondary structure

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456

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

13 – 28

16

Beta strand

34 – 44

11

Helix

48 – 51

4

Helix

59 – 63

5

Helix

64 – 71

8

Beta strand

76 – 81

6

Turn

84 – 86

3

Helix

90 – 96

7

Beta strand

97 – 102

6

Turn

115 – 118

4

Beta strand

122 – 124

3

Helix

125 – 132

8

Helix

136 – 138

3

Beta strand

147 – 153

7

Helix

157 – 167

11

Helix

170 – 173

4

Helix

180 – 186

7

Beta strand

193 – 197

5

Helix

202 – 204

3

Helix

209 – 214

6

Helix

215 – 217

3

Beta strand

221 – 224

4

Helix

227 – 230

4

Helix

235 – 241

7

Helix

243 – 256

14

Beta strand

264 – 270

7

Beta strand

272 – 279

8

Beta strand

281 – 283

3

Beta strand

286 – 296

11

Beta strand

298 – 314

17

Beta strand

316 – 320

5

Turn

336 – 339

4

Beta strand

352 – 356

5

Helix

359 – 362

4

Helix

368 – 370

3

Helix

371 – 391

21

Helix

402 – 413

12

Helix

420 – 434

15

Helix

435 – 437

3

Helix

447 – 454

8

Sequences

	Sequence		Length	Mass (Da)
	O05783-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 74D91282BD78BFB9	FASTA	456	49,341
	10 20 30 40 50 60 MRPYYIAIVG SGPSAFFAAA SLLKAADTTE DLDMAVDMLE MLPTPWGLVR SGVAPDHPKI 70 80 90 100 110 120 KSISKQFEKT AEDPRFRFFG NVVVGEHVQP GELSERYDAV IYAVGAQSDR MLNIPGEDLP 130 140 150 160 170 180 GSIAAVDFVG WYNAHPHFEQ VSPDLSGARA VVIGNGNVAL DVARILLTDP DVLARTDIAD 190 200 210 220 230 240 HALESLRPRG IQEVVIVGRR GPLQAAFTTL ELRELADLDG VDVVIDPAEL DGITDEDAAA 250 260 270 280 290 300 VGKVCKQNIK VLRGYADREP RPGHRRMVFR FLTSPIEIKG KRKVERIVLG RNELVSDGSG 310 320 330 340 350 360 RVAAKDTGER EELPAQLVVR SVGYRGVPTP GLPFDDQSGT IPNVGGRING SPNEYVVGWI 370 380 390 400 410 420 KRGPTGVIGT NKKDAQDTVD TLIKNLGNAK EGAECKSFPE DHADQVADWL AARQPKLVTS 430 440 450 AHWQVIDAFE RAAGEPHGRP RVKLASLAEL LRIGLG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Mycobacterium tuberculosis FprA, a novel bacterial NADPH-ferredoxin reductase." Fischer F., Raimondi D., Aliverti A., Zanetti G. Eur. J. Biochem. 269:3005-3013(2002) [PubMed: 12071965] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21, CHARACTERIZATION.
[4]	"Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin reductase homologue FprA." McLean K.J., Scrutton N.S., Munro A.W. Biochem. J. 372:317-327(2003) [PubMed: 12614197] [Abstract] Cited for: ENZYME KINETICS, REDOX POTENTIOMETRY, ABSORPTION SPECTROSCOPY, CIRCULAR DICHROISM ANALYSIS, EPR SPECTROSCOPY.
[5]	"A covalent modification of NADP+ revealed by the atomic resolution structure of FprA, a Mycobacterium tuberculosis oxidoreductase." Bossi R.T., Aliverti A., Raimondi D., Fischer F., Zanetti G., Ferrari D., Tahallah N., Maier C.S., Heck A.J., Rizzi M., Mattevi A. Biochemistry 41:8807-8818(2002) [PubMed: 12102623] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.
[6]	"Role of the His57-Glu214 ionic couple located in the active site of Mycobacterium tuberculosis FprA." Pennati A., Razeto A., de Rosa M., Pandini V., Vanoni M.A., Mattevi A., Coda A., Aliverti A., Zanetti G. Biochemistry 45:8712-8720(2006) [PubMed: 16846214] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT GLN-57 IN COMPLEX WITH FAD AND NADPH, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

BX842582 Genomic DNA. Translation: CAB08363.1.
AE000516 Genomic DNA. Translation: AAK47528.1.

PIR

A70920.

RefSeq

NP_217622.1.
NP_337714.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LQT	X-ray	1.05	A/B	1-456	[»]
1LQU	X-ray	1.25	A/B	1-456	[»]
2C7G	X-ray	1.80	A	1-456	[»]

ModBase

Search...

Genome annotation databases

GeneID

888839.
926712.

GenomeReviews

Gene locus MT3189 in contig AE000516_GR.
Gene locus Rv3106 in contig AL123456_GR.

KEGG

mtc:MT3189.
mtu:Rv3106.

TIGR

MT3189.

Organism-specific databases

TubercuList

Rv3106.

Phylogenomic databases

HOGENOM

O05783.

OMA

O05783. YHAVLLT.

Enzyme and pathway databases

BRENDA

1.18.1.2. 809.

Family and domain databases

InterPro

IPR000759. Adrndx_reductase.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
[Graphical view]

Pfam

PF07992. Pyr_redox_2. 1 hit.
[Graphical view]

PRINTS

PR00419. ADXRDTASE.

ProtoNet

Search...

Entry information

Entry name

FPRA_MYCTU

Accession

Primary (citable) accession number: O05783

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)