Reviewed, UniProtKB/Swiss-Prot P0C186 (PNTAA_RHORU)

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

Organism

Rhodospirillum rubrum

Taxonomic identifier

1085 [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.
Sequence similarities	Belongs to the AlaDH/PNT family.

Ontologies

Keywords
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
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_0000199019

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 – 29

10

Beta strand

32 – 36

5

Turn

37 – 44

8

Helix

47 – 52

6

Beta strand

55 – 60

6

Helix

61 – 65

5

Beta strand

69 – 72

4

Helix

80 – 82

3

Helix

87 – 89

3

Beta strand

95 – 98

4

Turn

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

308 – 312

5

Beta strand

315 – 319

5

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

Sequences

	Sequence		Length	Mass (Da)
	P0C186-1 [UniParc]. Last modified April 4, 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

[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]	"Protein-protein recognition, hydride transfer and proton pumping in the transhydrogenase complex." Buckley P.A., Jackson J.B., Schneider T., White S.A., Rice D.W., Baker P.J. Structure 8:809-815(2000) [PubMed: 10997900] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U01158 Genomic DNA. Translation: AAC43255.1.

PIR

S69123.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FR8	X-ray	2.60	A/B	1-384	[»]
2FRD	X-ray	3.20	A/B	1-384	[»]
2FSV	X-ray	2.30	A/B	1-384	[»]
2OO5	X-ray	2.60	A/B	1-384	[»]
2OOR	X-ray	2.32	A/B	1-384	[»]

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

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_RHORU

Accession

Primary (citable) accession number: P0C186
Secondary accession number(s): Q60164

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	April 4, 2006
Last modified:	June 16, 2009
This is version 26 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)