Reviewed, UniProtKB/Swiss-Prot P0C188 (PNTB_RHORU)

Names and origin

Protein names

Recommended name:
    NAD(P) transhydrogenase subunit beta
    EC=1.6.1.2
Alternative name(s):
    Nicotinamide nucleotide transhydrogenase subunit beta
    Pyridine nucleotide transhydrogenase subunit beta
    Proton-translocating transhydrogenase NADP(H)-binding component
    dIII

Gene names

Name:	pntB
Synonyms:	nntB

Organism

Rhodospirillum rubrum

Taxonomic identifier

1085 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Rhodospirillum

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane By similarity.
Catalytic activity	NADPH + NAD+ = NADP+ + NADH.
Subunit structure	Complex of an alpha and a beta chain; in Rhodospirillum, the alpha chain seems to be made of two subunits.
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the PNT beta subunit family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD(P)+ transhydrogenase (AB-specific) activity Inferred from electronic annotation. Source: EC NADP or NADPH binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 464

464

NAD(P) transhydrogenase subunit beta

PRO_0000199027

Regions

Transmembrane

54 – 74

21

Potential

Transmembrane

86 – 106

21

Potential

Transmembrane

126 – 146

21

Potential

Transmembrane

164 – 184

21

Potential

Transmembrane

191 – 211

21

Potential

Transmembrane

227 – 247

21

Potential

Secondary structure

1

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464

Helix Strand Turn

Details...

Helix

297 – 306

10

Beta strand

308 – 314

7

Helix

316 – 321

6

Helix

324 – 336

13

Beta strand

340 – 345

6

Beta strand

350 – 352

3

Helix

355 – 362

8

Helix

367 – 369

3

Beta strand

370 – 372

3

Helix

373 – 376

4

Helix

377 – 379

3

Beta strand

384 – 390

7

Helix

393 – 395

3

Helix

397 – 399

3

Turn

406 – 409

4

Helix

415 – 417

3

Beta strand

418 – 428

11

Helix

438 – 441

4

Beta strand

445 – 450

6

Helix

452 – 462

11

Sequences

	Sequence		Length	Mass (Da)
	P0C188-1 [UniParc]. Last modified April 4, 2006. Version 1. Checksum: 79200D4F8861779B	FASTA	464	47,808
	10 20 30 40 50 60 MTHSLTMAAY IVAGVLFILA LRGLSNPESA RNGNRMGMVG MAIAILTTLL SPSVQAYAWI 70 80 90 100 110 120 VLAIAIGGAI GTVIAKKVLM TALPQLVAAF HSLVGMAAVL VATGALLNPE AYGIGSAGAI 130 140 150 160 170 180 HAGSLVEMSL GLAVGAITFS GSVIAFGKLQ GLIAGKPVTF PMQHPLNAVL GILLVVLLVV 190 200 210 220 230 240 FAATESHTAY FALMILAFAL GFLLIIPIGG ADMPVVISML NSYSGWAAAG IGFTLGNPLL 250 260 270 280 290 300 IIAGALVGSS GAILSYIMCK GMNRSIFNVI LGGFGSEGGV AAAGGAAGDR SVKAGSAEDA 310 320 330 340 350 360 AFIMKNASKV IIVPGYGMAV AQAQHALREM ADVLKKEGVE VSYAIHPVAG RMPGHMNVLL 370 380 390 400 410 420 AEANVPYDEV FELEEINSSF QTADVAFVIG ANDVTNPAAK TDPSSPIYGM PILDVEKAGT 430 440 450 460 VLFIKRSMAS GYAGVENELF FRNNTMMLFG DAKKMTEQIV QAMN

References

[1]	"Energy-transducing nicotinamide nucleotide transhydrogenase: nucleotide sequences of the genes and predicted amino acid sequences of the subunits of the enzyme from Rhodospirillum rubrum." Yamaguchi M., Hatefi Y. J. Bioenerg. Biomembr. 26:435-445(1994) [PubMed: 7844118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum." Jeeves M., Smith K.J., Quirk P.G., Cotton N.P.J., Jackson J.B. Biochim. Biophys. Acta 1459:248-257(2000) [PubMed: 11004437] [Abstract] Cited for: STRUCTURE BY NMR OF 262-464.
[3]	"The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase." Cotton N.P.J., White S.A., Peake S.J., McSweeney S., Baz Jackson J. Structure 9:165-176(2001) [PubMed: 11250201] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 262-464.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U01158 Genomic DNA. Translation: AAC43257.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FR8	X-ray	2.60	C	262-464	[»]
2FRD	X-ray	3.20	C	262-464	[»]
2FSV	X-ray	2.30	C	262-464	[»]
2OO5	X-ray	2.60	C	291-464	[»]
2OOR	X-ray	2.32	C	291-464	[»]

ModBase

Search...

Protein family/group databases

TCDB

3.D.2.2.1. proton-translocating transhydrogenase (PTH) family.

Enzyme and pathway databases

BRENDA

1.6.1.2. 1671.

Family and domain databases

InterPro

IPR012136. NADH_DH_b.
IPR004003. NADP_transhyd_b.
[Graphical view]

Pfam

PF02233. PNTB. 1 hit.
[Graphical view]

PIRSF

PIRSF000204. PNTB. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PNTB_RHORU

Accession

Primary (citable) accession number: P0C188
Secondary accession number(s): Q59763, Q59765

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	April 4, 2006
Last modified:	June 16, 2009
This is version 25 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)