Reviewed, UniProtKB/Swiss-Prot Q2RSB2 (PNTAA_RHORT)

Names and origin

Protein names

Recommended name:
    NAD(P) transhydrogenase subunit alpha part 1
    EC=1.6.1.2
Alternative name(s):
    Nicotinamide nucleotide transhydrogenase subunit alpha 1
    Pyridine nucleotide transhydrogenase subunit alpha 1
    Proton-translocating transhydrogenase component 1
    dI

Gene names

Name:	pntAA
Synonyms:	nntA1
Ordered Locus Names:	Rru_A2183

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	384 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.
Sequence similarities	Belongs to the AlaDH/PNT family.

Ontologies

Keywords
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
Molecular function	NAD(P)+ transhydrogenase (AB-specific) activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro electron carrier activity 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 – 384

384

NAD(P) transhydrogenase subunit alpha part 1

PRO_0000231663

Regions

Nucleotide binding

167 – 197

31

NAD By similarity

Secondary structure

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384

Helix Strand Turn

Details...

Beta strand

2 – 5

4

Helix

20 – 28

9

Beta strand

32 – 36

5

Turn

37 – 40

4

Helix

41 – 43

3

Helix

47 – 53

7

Beta strand

56 – 60

5

Helix

61 – 65

5

Beta strand

69 – 75

7

Helix

80 – 82

3

Helix

87 – 89

3

Beta strand

95 – 99

5

Helix

102 – 104

3

Helix

106 – 114

9

Beta strand

118 – 121

4

Helix

122 – 124

3

Helix

129 – 134

6

Helix

136 – 155

20

Beta strand

163 – 165

3

Beta strand

168 – 170

3

Beta strand

174 – 178

5

Helix

182 – 193

12

Beta strand

197 – 201

5

Helix

207 – 213

7

Helix

241 – 255

15

Beta strand

259 – 263

5

Helix

278 – 282

5

Beta strand

289 – 292

4

Helix

295 – 297

3

Beta strand

309 – 312

4

Beta strand

315 – 318

4

Helix

323 – 327

5

Helix

328 – 343

16

Helix

344 – 346

3

Turn

349 – 352

4

Helix

361 – 366

6

Beta strand

367 – 370

4

Helix

377 – 379

3

Sequences

	Sequence		Length	Mass (Da)
	Q2RSB2-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: B886A640CE2BFA12	FASTA	384	40,277
	10 20 30 40 50 60 MKIAIPKERR PGEDRVAISP EVVKKLVGLG FEVIVEQGAG VGASITDDAL TAAGATIAST 70 80 90 100 110 120 AAQALSQADV VWKVQRPMTA EEGTDEVALI KEGAVLMCHL GALTNRPVVE ALTKRKITAY 130 140 150 160 170 180 AMELMPRISR AQSMDILSSQ SNLAGYRAVI DGAYEFARAF PMMMTAAGTV PPARVLVFGV 190 200 210 220 230 240 GVAGLQAIAT AKRLGAVVMA TDVRAATKEQ VESLGGKFIT VDDEAMKTAE TAGGYAKEMG 250 260 270 280 290 300 EEFRKKQAEA VLKELVKTDI AITTALIPGK PAPVLITEEM VTKMKPGSVI IDLAVEAGGN 310 320 330 340 350 360 CPLSEPGKIV VKHGVKIVGH TNVPSRVAAD ASPLFAKNLL NFLTPHVDKD TKTLVMKLED 370 380 ETVSGTCVTR DGAIVHPALT GQGA

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: AAA62493.1.
CP000230 Genomic DNA. Translation: ABC22983.1.

RefSeq

YP_427270.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F8G	X-ray	2.00	A/B/C/D	1-384	[»]
1HZZ	X-ray	2.50	A/B	1-384	[»]
1L7D	X-ray	1.81	A/B/C/D	1-384	[»]
1L7E	X-ray	1.90	A/B/C/D	1-384	[»]
1NM5	X-ray	2.40	A/B	1-384	[»]
1PTJ	X-ray	2.61	A/B	1-381	[»]
1U28	X-ray	2.30	A/B	1-384	[»]
1U2D	X-ray	3.00	A/B	1-384	[»]
1U2G	X-ray	2.20	A/B	1-384	[»]
1XLT	X-ray	3.10	A/B/D/E/G/H	1-384	[»]

ModBase

Search...

Genome annotation databases

GeneID

3835610.

GenomeReviews

Gene locus Rru_A2183 in contig CP000230_GR.

KEGG

rru:Rru_A2183.

NMPDR

fig|1085.1.peg.3658.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q2RSB2.

OMA

Q2RSB2. EAENTET.

Enzyme and pathway databases

BioCyc

RRUB269796:RRU_A2183-MON.

Family and domain databases

InterPro

IPR007698. Ala_DH/PNT_C.
IPR008142. Ala_DH/PNT_CS1.
IPR008143. Ala_DH/PNT_CS2.
IPR007886. Ala_DH/PNT_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
[Graphical view]

PROSITE

PS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PNTAA_RHORT

Accession

Primary (citable) accession number: Q2RSB2
Secondary accession number(s): Q60164

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	January 24, 2006
Last modified:	June 16, 2009
This is version 30 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)