Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NAD(P) transhydrogenase subunit beta

Gene

pntB

Organism
Rhodospirillum rubrum
Status
Reviewed-Annotation score: Annotation score: 3 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.

GO - Molecular functioni

GO - Biological processi

  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-3684-MONOMER.

Protein family/group databases

TCDBi3.D.2.2.1. the proton-translocating transhydrogenase (pth) family.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P) transhydrogenase subunit beta (EC:1.6.1.2)
Alternative name(s):
Nicotinamide nucleotide transhydrogenase subunit beta
Proton-translocating transhydrogenase NADP(H)-binding component
Pyridine nucleotide transhydrogenase subunit beta
dIII
Gene namesi
Name:pntB
Synonyms:nntB
OrganismiRhodospirillum rubrum
Taxonomic identifieri1085 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei54 – 7421HelicalSequence analysisAdd
BLAST
Transmembranei86 – 10621HelicalSequence analysisAdd
BLAST
Transmembranei126 – 14621HelicalSequence analysisAdd
BLAST
Transmembranei164 – 18421HelicalSequence analysisAdd
BLAST
Transmembranei191 – 21121HelicalSequence analysisAdd
BLAST
Transmembranei227 – 24721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464NAD(P) transhydrogenase subunit betaPRO_0000199027Add
BLAST

Interactioni

Subunit structurei

Complex of an alpha and a beta chain; in Rhodospirillum, the alpha chain seems to be made of two subunits.

Protein-protein interaction databases

STRINGi269796.Rru_A2181.

Structurei

Secondary structure

1
464
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi297 – 30610Combined sources
Beta strandi308 – 3147Combined sources
Helixi316 – 3216Combined sources
Helixi324 – 33613Combined sources
Beta strandi340 – 3456Combined sources
Beta strandi350 – 3523Combined sources
Helixi355 – 3628Combined sources
Helixi367 – 3693Combined sources
Beta strandi370 – 3723Combined sources
Helixi373 – 3764Combined sources
Helixi377 – 3793Combined sources
Beta strandi384 – 3907Combined sources
Helixi393 – 3953Combined sources
Helixi397 – 3993Combined sources
Turni406 – 4094Combined sources
Helixi415 – 4173Combined sources
Beta strandi418 – 42811Combined sources
Helixi438 – 4414Combined sources
Beta strandi445 – 4506Combined sources
Helixi452 – 46211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FR8X-ray2.60C262-464[»]
2FRDX-ray3.20C262-464[»]
2FSVX-ray2.30C262-464[»]
2OO5X-ray2.60C291-464[»]
2OORX-ray2.32C291-464[»]
ProteinModelPortaliP0C188.
SMRiP0C188. Positions 290-464.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C188.

Family & Domainsi

Sequence similaritiesi

Belongs to the PNT beta subunit family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C15. Bacteria.
COG1282. LUCA.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR012136. NADH_DH_b.
[Graphical view]
PfamiPF02233. PNTB. 1 hit.
[Graphical view]
PIRSFiPIRSF000204. PNTB. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.

Sequencei

Sequence statusi: Complete.

P0C188-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHSLTMAAY IVAGVLFILA LRGLSNPESA RNGNRMGMVG MAIAILTTLL
60 70 80 90 100
SPSVQAYAWI VLAIAIGGAI GTVIAKKVLM TALPQLVAAF HSLVGMAAVL
110 120 130 140 150
VATGALLNPE AYGIGSAGAI HAGSLVEMSL GLAVGAITFS GSVIAFGKLQ
160 170 180 190 200
GLIAGKPVTF PMQHPLNAVL GILLVVLLVV FAATESHTAY FALMILAFAL
210 220 230 240 250
GFLLIIPIGG ADMPVVISML NSYSGWAAAG IGFTLGNPLL IIAGALVGSS
260 270 280 290 300
GAILSYIMCK GMNRSIFNVI LGGFGSEGGV AAAGGAAGDR SVKAGSAEDA
310 320 330 340 350
AFIMKNASKV IIVPGYGMAV AQAQHALREM ADVLKKEGVE VSYAIHPVAG
360 370 380 390 400
RMPGHMNVLL AEANVPYDEV FELEEINSSF QTADVAFVIG ANDVTNPAAK
410 420 430 440 450
TDPSSPIYGM PILDVEKAGT VLFIKRSMAS GYAGVENELF FRNNTMMLFG
460
DAKKMTEQIV QAMN
Length:464
Mass (Da):47,808
Last modified:April 4, 2006 - v1
Checksum:i79200D4F8861779B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01158 Genomic DNA. Translation: AAC43257.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01158 Genomic DNA. Translation: AAC43257.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FR8X-ray2.60C262-464[»]
2FRDX-ray3.20C262-464[»]
2FSVX-ray2.30C262-464[»]
2OO5X-ray2.60C291-464[»]
2OORX-ray2.32C291-464[»]
ProteinModelPortaliP0C188.
SMRiP0C188. Positions 290-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269796.Rru_A2181.

Protein family/group databases

TCDBi3.D.2.2.1. the proton-translocating transhydrogenase (pth) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C15. Bacteria.
COG1282. LUCA.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-3684-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0C188.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR012136. NADH_DH_b.
[Graphical view]
PfamiPF02233. PNTB. 1 hit.
[Graphical view]
PIRSFiPIRSF000204. PNTB. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 262-464.

Entry informationi

Entry nameiPNTB_RHORU
AccessioniPrimary (citable) accession number: P0C188
Secondary accession number(s): Q59763, Q59765
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: November 11, 2015
This is version 54 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

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.