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Protein

NAD(P) transhydrogenase subunit alpha part 1

Gene

pntAA

Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

NADPH + NAD+ = NADP+ + NADH.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei234NAD; via carbonyl oxygen3 Publications1
Binding sitei247NAD3 Publications1
Binding sitei266NAD; via carbonyl oxygen3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi127 – 129NAD3 Publications3
Nucleotide bindingi132 – 135NAD3 Publications4
Nucleotide bindingi180 – 182NAD3 Publications3
Nucleotide bindingi202 – 204NAD3 Publications3

GO - Molecular functioni

  • NAD(P)+ transhydrogenase (AB-specific) activity Source: UniProtKB
  • NAD(P)+ transhydrogenase (B-specific) activity Source: CACAO
  • NAD+ binding Source: UniProtKB
  • NAD binding Source: UniProtKB
  • NADH binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB

GO - Biological processi

  • NADPH regeneration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.6.1.2. 5420.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P) transhydrogenase subunit alpha part 1 (EC:1.6.1.2)
Alternative name(s):
Nicotinamide nucleotide transhydrogenase subunit alpha 1
Proton-translocating transhydrogenase component 1
Pyridine nucleotide transhydrogenase subunit alpha 1
dI
Gene namesi
Name:pntAA
Synonyms:nntA1
Ordered Locus Names:Rru_A2183
OrganismiRhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Taxonomic identifieri269796 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum
Proteomesi
  • UP000001929 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi127R → A or M: No effect on interaction with PntB, but hydride transfer inhibited. Much weaker binding to NADH. 1 Publication1
Mutagenesisi132Q → N: No effect on interaction with PntB, but hydride transfer strongly inhibited. No effect on NADH binding affinity on its own, but differences in NADH binding properties in complex with PntB. 1 Publication1
Mutagenesisi135D → N: No effect on interaction with PntB, but hydride transfer strongly inhibited. No effect on the binding affinity to NADH. 1 Publication1
Mutagenesisi138S → A: No effect on interaction with PntB, but hydride transfer strongly inhibited. No effect on the binding affinity to NADH. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002316631 – 384NAD(P) transhydrogenase subunit alpha part 1Add BLAST384

Proteomic databases

PRIDEiQ2RSB2.

Interactioni

Subunit structurei

Heterotrimer of two alpha chains and a beta (PntB) chain; in Rhodospirillum, the alpha chain is made of two subunits (PntAA and PntAB) and forms a dimer.5 Publications

GO - Molecular functioni

  • protein dimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi269796.Rru_A2183.

Structurei

Secondary structure

1384
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Beta strandi10 – 12Combined sources3
Helixi20 – 28Combined sources9
Beta strandi32 – 36Combined sources5
Turni37 – 40Combined sources4
Helixi41 – 43Combined sources3
Helixi47 – 52Combined sources6
Beta strandi56 – 60Combined sources5
Helixi61 – 65Combined sources5
Beta strandi69 – 75Combined sources7
Helixi80 – 82Combined sources3
Helixi86 – 89Combined sources4
Beta strandi95 – 99Combined sources5
Helixi102 – 104Combined sources3
Helixi106 – 114Combined sources9
Beta strandi118 – 121Combined sources4
Helixi122 – 124Combined sources3
Helixi129 – 134Combined sources6
Helixi136 – 155Combined sources20
Beta strandi163 – 165Combined sources3
Beta strandi168 – 170Combined sources3
Beta strandi174 – 178Combined sources5
Helixi182 – 193Combined sources12
Beta strandi197 – 201Combined sources5
Helixi208 – 213Combined sources6
Turni223 – 228Combined sources6
Beta strandi233 – 235Combined sources3
Helixi247 – 255Combined sources9
Beta strandi259 – 263Combined sources5
Beta strandi268 – 270Combined sources3
Helixi278 – 281Combined sources4
Beta strandi289 – 292Combined sources4
Helixi295 – 297Combined sources3
Beta strandi309 – 312Combined sources4
Beta strandi315 – 318Combined sources4
Helixi323 – 327Combined sources5
Helixi328 – 343Combined sources16
Helixi344 – 346Combined sources3
Turni349 – 352Combined sources4
Beta strandi358 – 360Combined sources3
Helixi361 – 366Combined sources6
Beta strandi367 – 370Combined sources4
Beta strandi371 – 374Combined sources4
Beta strandi379 – 381Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F8GX-ray2.00A/B/C/D1-384[»]
1HZZX-ray2.50A/B1-384[»]
1L7DX-ray1.81A/B/C/D1-384[»]
1L7EX-ray1.90A/B/C/D1-384[»]
1NM5X-ray2.40A/B1-384[»]
1PTJX-ray2.61A/B1-381[»]
1U28X-ray2.30A/B1-384[»]
1U2DX-ray3.00A/B1-384[»]
1U2GX-ray2.20A/B1-384[»]
1XLTX-ray3.10A/B/D/E/G/H1-384[»]
2FR8X-ray2.60A/B1-384[»]
2FRDX-ray3.20A/B1-384[»]
2FSVX-ray2.30A/B1-384[»]
2OO5X-ray2.60A/B1-384[»]
2OORX-ray2.32A/B1-384[»]
ProteinModelPortaliQ2RSB2.
SMRiQ2RSB2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2RSB2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 136RQD loop; involved in interaction with PntBAdd BLAST11

Sequence similaritiesi

Belongs to the AlaDH/PNT family.Curated

Phylogenomic databases

eggNOGiENOG4108IIE. Bacteria.
COG3288. LUCA.
HOGENOMiHOG000022121.
KOiK00324.
OMAiDSCVTRE.
OrthoDBiPOG091H0397.

Family and domain databases

InterProiIPR008143. Ala_DH/PNT_CS2.
IPR008142. AlaDH/PNT_CS1.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
[Graphical view]
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2RSB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIAIPKERR PGEDRVAISP EVVKKLVGLG FEVIVEQGAG VGASITDDAL
60 70 80 90 100
TAAGATIAST AAQALSQADV VWKVQRPMTA EEGTDEVALI KEGAVLMCHL
110 120 130 140 150
GALTNRPVVE ALTKRKITAY AMELMPRISR AQSMDILSSQ SNLAGYRAVI
160 170 180 190 200
DGAYEFARAF PMMMTAAGTV PPARVLVFGV GVAGLQAIAT AKRLGAVVMA
210 220 230 240 250
TDVRAATKEQ VESLGGKFIT VDDEAMKTAE TAGGYAKEMG EEFRKKQAEA
260 270 280 290 300
VLKELVKTDI AITTALIPGK PAPVLITEEM VTKMKPGSVI IDLAVEAGGN
310 320 330 340 350
CPLSEPGKIV VKHGVKIVGH TNVPSRVAAD ASPLFAKNLL NFLTPHVDKD
360 370 380
TKTLVMKLED ETVSGTCVTR DGAIVHPALT GQGA
Length:384
Mass (Da):40,277
Last modified:January 24, 2006 - v1
Checksum:iB886A640CE2BFA12
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05294 Genomic DNA. Translation: AAA62493.1.
CP000230 Genomic DNA. Translation: ABC22983.1.
RefSeqiWP_011390032.1. NC_007643.1.
YP_427270.1. NC_007643.1.

Genome annotation databases

EnsemblBacteriaiABC22983; ABC22983; Rru_A2183.
GeneIDi3835610.
KEGGirru:Rru_A2183.
PATRICi23328064. VBIRhoRub82919_2277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05294 Genomic DNA. Translation: AAA62493.1.
CP000230 Genomic DNA. Translation: ABC22983.1.
RefSeqiWP_011390032.1. NC_007643.1.
YP_427270.1. NC_007643.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F8GX-ray2.00A/B/C/D1-384[»]
1HZZX-ray2.50A/B1-384[»]
1L7DX-ray1.81A/B/C/D1-384[»]
1L7EX-ray1.90A/B/C/D1-384[»]
1NM5X-ray2.40A/B1-384[»]
1PTJX-ray2.61A/B1-381[»]
1U28X-ray2.30A/B1-384[»]
1U2DX-ray3.00A/B1-384[»]
1U2GX-ray2.20A/B1-384[»]
1XLTX-ray3.10A/B/D/E/G/H1-384[»]
2FR8X-ray2.60A/B1-384[»]
2FRDX-ray3.20A/B1-384[»]
2FSVX-ray2.30A/B1-384[»]
2OO5X-ray2.60A/B1-384[»]
2OORX-ray2.32A/B1-384[»]
ProteinModelPortaliQ2RSB2.
SMRiQ2RSB2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269796.Rru_A2183.

Proteomic databases

PRIDEiQ2RSB2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC22983; ABC22983; Rru_A2183.
GeneIDi3835610.
KEGGirru:Rru_A2183.
PATRICi23328064. VBIRhoRub82919_2277.

Phylogenomic databases

eggNOGiENOG4108IIE. Bacteria.
COG3288. LUCA.
HOGENOMiHOG000022121.
KOiK00324.
OMAiDSCVTRE.
OrthoDBiPOG091H0397.

Enzyme and pathway databases

BRENDAi1.6.1.2. 5420.

Miscellaneous databases

EvolutionaryTraceiQ2RSB2.
PROiQ2RSB2.

Family and domain databases

InterProiIPR008143. Ala_DH/PNT_CS2.
IPR008142. AlaDH/PNT_CS1.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
[Graphical view]
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPNTAA_RHORT
AccessioniPrimary (citable) accession number: Q2RSB2
Secondary accession number(s): Q60164
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 24, 2006
Last modified: November 2, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.