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Protein

NAD(P) transhydrogenase subunit beta

Gene

pntB

Organism
Escherichia coli (strain K12)
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.

Catalytic activityi

NADPH + NAD+ = NADP+ + NADH.

GO - Molecular functioni

  • NAD(P)+ transhydrogenase (AB-specific) activity Source: EcoCyc
  • NAD(P)+ transhydrogenase activity Source: EcoCyc
  • NADP binding Source: EcoCyc

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciEcoCyc:PNTB-MONOMER.
ECOL316407:JW1594-MONOMER.
MetaCyc:PNTB-MONOMER.

Protein family/group databases

TCDBi3.D.2.1.1. 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
Pyridine nucleotide transhydrogenase subunit beta
Gene namesi
Name:pntB
Ordered Locus Names:b1602, JW1594
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10745. pntB.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33PeriplasmicSequence analysis
Transmembranei4 – 2421HelicalSequence analysisAdd
BLAST
Topological domaini25 – 4521CytoplasmicSequence analysisAdd
BLAST
Transmembranei46 – 6621HelicalSequence analysisAdd
BLAST
Topological domaini67 – 8216PeriplasmicSequence analysisAdd
BLAST
Transmembranei83 – 10321HelicalSequence analysisAdd
BLAST
Topological domaini104 – 11512CytoplasmicSequence analysisAdd
BLAST
Transmembranei116 – 13621HelicalSequence analysisAdd
BLAST
Topological domaini137 – 16428PeriplasmicSequence analysisAdd
BLAST
Transmembranei165 – 18521HelicalSequence analysisAdd
BLAST
Topological domaini186 – 1883CytoplasmicSequence analysis
Transmembranei189 – 20921HelicalSequence analysisAdd
BLAST
Topological domaini210 – 2156PeriplasmicSequence analysis
Transmembranei216 – 23621HelicalSequence analysisAdd
BLAST
Topological domaini237 – 2393CytoplasmicSequence analysis
Transmembranei240 – 26021HelicalSequence analysisAdd
BLAST
Topological domaini261 – 30848PeriplasmicSequence analysisAdd
BLAST
Transmembranei309 – 32921HelicalSequence analysisAdd
BLAST
Topological domaini330 – 462133CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462NAD(P) transhydrogenase subunit betaPRO_0000199023Add
BLAST

Proteomic databases

PaxDbiP0AB67.
PRIDEiP0AB67.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

BioGridi4259125. 16 interactions.
DIPiDIP-367N.
STRINGi511145.b1602.

Structurei

Secondary structure

1
462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi297 – 3059Combined sources
Beta strandi307 – 3126Combined sources
Helixi316 – 3194Combined sources
Turni320 – 3223Combined sources
Helixi323 – 33614Combined sources
Beta strandi339 – 3446Combined sources
Beta strandi346 – 3538Combined sources
Helixi355 – 3628Combined sources
Turni366 – 3683Combined sources
Beta strandi369 – 3724Combined sources
Helixi376 – 3816Combined sources
Beta strandi383 – 3875Combined sources
Helixi391 – 3944Combined sources
Helixi396 – 3983Combined sources
Beta strandi404 – 4063Combined sources
Beta strandi417 – 4237Combined sources
Beta strandi425 – 4273Combined sources
Turni437 – 4393Combined sources
Beta strandi440 – 4478Combined sources
Helixi451 – 46111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BRUNMR-C286-462[»]
ProteinModelPortaliP0AB67.
SMRiP0AB67. Positions 5-462.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AB67.

Family & Domainsi

Sequence similaritiesi

Belongs to the PNT beta subunit family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C15. Bacteria.
COG1282. LUCA.
HOGENOMiHOG000243958.
InParanoidiP0AB67.
KOiK00325.
OMAiHHAEVFI.
PhylomeDBiP0AB67.

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.

P0AB67-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGLVTAAY IVAAILFIFS LAGLSKHETS RQGNNFGIAG MAIALIATIF
60 70 80 90 100
GPDTGNVGWI LLAMVIGGAI GIRLAKKVEM TEMPELVAIL HSFVGLAAVL
110 120 130 140 150
VGFNSYLHHD AGMAPILVNI HLTEVFLGIF IGAVTFTGSV VAFGKLCGKI
160 170 180 190 200
SSKPLMLPNR HKMNLAALVV SFLLLIVFVR TDSVGLQVLA LLIMTAIALV
210 220 230 240 250
FGWHLVASIG GADMPVVVSM LNSYSGWAAA AAGFMLSNDL LIVTGALVGS
260 270 280 290 300
SGAILSYIMC KAMNRSFISV IAGGFGTDGS STGDDQEVGE HREITAEETA
310 320 330 340 350
ELLKNSHSVI ITPGYGMAVA QAQYPVAEIT EKLRARGINV RFGIHPVAGR
360 370 380 390 400
LPGHMNVLLA EAKVPYDIVL EMDEINDDFA DTDTVLVIGA NDTVNPAAQD
410 420 430 440 450
DPKSPIAGMP VLEVWKAQNV IVFKRSMNTG YAGVQNPLFF KENTHMLFGD
460
AKASVDAILK AL
Length:462
Mass (Da):48,723
Last modified:November 8, 2005 - v1
Checksum:iD11747291D271A2F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04195 Genomic DNA. Translation: CAB37090.1.
X66086 Genomic DNA. Translation: CAA46885.1.
U00096 Genomic DNA. Translation: AAC74674.1.
AP009048 Genomic DNA. Translation: BAA15336.1.
PIRiS24381. DEECXB.
RefSeqiNP_416119.1. NC_000913.3.
WP_000014036.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74674; AAC74674; b1602.
BAA15336; BAA15336; BAA15336.
GeneIDi946144.
KEGGiecj:JW1594.
eco:b1602.
PATRICi32118506. VBIEscCol129921_1673.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04195 Genomic DNA. Translation: CAB37090.1.
X66086 Genomic DNA. Translation: CAA46885.1.
U00096 Genomic DNA. Translation: AAC74674.1.
AP009048 Genomic DNA. Translation: BAA15336.1.
PIRiS24381. DEECXB.
RefSeqiNP_416119.1. NC_000913.3.
WP_000014036.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BRUNMR-C286-462[»]
ProteinModelPortaliP0AB67.
SMRiP0AB67. Positions 5-462.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259125. 16 interactions.
DIPiDIP-367N.
STRINGi511145.b1602.

Protein family/group databases

TCDBi3.D.2.1.1. the proton-translocating transhydrogenase (pth) family.

Proteomic databases

PaxDbiP0AB67.
PRIDEiP0AB67.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74674; AAC74674; b1602.
BAA15336; BAA15336; BAA15336.
GeneIDi946144.
KEGGiecj:JW1594.
eco:b1602.
PATRICi32118506. VBIEscCol129921_1673.

Organism-specific databases

EchoBASEiEB0738.
EcoGeneiEG10745. pntB.

Phylogenomic databases

eggNOGiENOG4105C15. Bacteria.
COG1282. LUCA.
HOGENOMiHOG000243958.
InParanoidiP0AB67.
KOiK00325.
OMAiHHAEVFI.
PhylomeDBiP0AB67.

Enzyme and pathway databases

BioCyciEcoCyc:PNTB-MONOMER.
ECOL316407:JW1594-MONOMER.
MetaCyc:PNTB-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AB67.
PROiP0AB67.

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...

Entry informationi

Entry nameiPNTB_ECOLI
AccessioniPrimary (citable) accession number: P0AB67
Secondary accession number(s): P07002, P76890
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 8, 2005
Last modified: September 7, 2016
This is version 91 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, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.