Reviewed, UniProtKB/Swiss-Prot Q2RSB4 (PNTB_RHORT)

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
Ordered Locus Names:	Rru_A2181

Organism

Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255) [Complete proteome] [HAMAP]

Taxonomic identifier

269796 [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 By similarity.
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 Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
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_0000231665

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 – 305

9

Beta strand

308 – 314

7

Helix

316 – 321

6

Helix

324 – 334

11

Turn

335 – 338

4

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

379 – 382

4

Beta strand

384 – 390

7

Turn

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 – 463

12

Sequences

	Sequence		Length	Mass (Da)
	Q2RSB4-1 [UniParc]. Last modified January 24, 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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of the genes for the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum and the implications for the domain structure of the enzyme." Williams R., Cotton N.P., Thomas C.M., Jackson J.B. Microbiology 140:1595-1604(1994) [PubMed: 8075801] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C. Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U05294 Genomic DNA. Translation: AAA62495.1.
CP000230 Genomic DNA. Translation: ABC22981.1.

RefSeq

YP_427268.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E3T	NMR	-	A	262-464	[»]
1HZZ	X-ray	2.50	C	262-464	[»]
1NM5	X-ray	2.40	C	262-464	[»]
1PNO	X-ray	2.10	A/B	294-464	[»]
1PNQ	X-ray	2.40	A/B	294-464	[»]
1PTJ	X-ray	2.61	C	291-464	[»]
1U28	X-ray	2.30	C	262-464	[»]
1U2D	X-ray	3.00	C	262-464	[»]
1U2G	X-ray	2.20	C	262-464	[»]
1XLT	X-ray	3.10	C/F/I	294-464	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q2RSB4.

Genome annotation databases

GeneID

3835608.

GenomeReviews

Gene locus Rru_A2181 in contig CP000230_GR.

KEGG

rru:Rru_A2181.

NMPDR

fig|1085.1.peg.3656.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q2RSB4.

OMA

QSWLPFI.

Enzyme and pathway databases

BioCyc

RRUB269796:RRU_A2181-MON.

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_RHORT

Accession

Primary (citable) accession number: Q2RSB4
Secondary accession number(s): Q59763, Q59765

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	January 24, 2006
Last modified:	November 3, 2009
This is version 32 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)