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Protein

NAD(P) transhydrogenase, mitochondrial

Gene

NNT

Organism
Bos taurus (Bovine)
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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi229 – 25931NADBy similarityAdd
BLAST
Nucleotide bindingi965 – 9706NADP
Nucleotide bindingi1007 – 10115NADP
Nucleotide bindingi1042 – 10498NADP
Nucleotide bindingi1068 – 10692NADP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

ReactomeiR-BTA-71403. Citric acid cycle (TCA cycle).

Protein family/group databases

TCDBi3.D.2.3.1. the proton-translocating transhydrogenase (pth) family.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P) transhydrogenase, mitochondrial (EC:1.6.1.2)
Alternative name(s):
Nicotinamide nucleotide transhydrogenase
Pyridine nucleotide transhydrogenase
Gene namesi
Name:NNT
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 20

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini44 – 474431Mitochondrial matrix1 PublicationAdd
BLAST
Transmembranei475 – 49319HelicalSequence analysisAdd
BLAST
Transmembranei501 – 52121HelicalSequence analysisAdd
BLAST
Transmembranei527 – 54620HelicalSequence analysisAdd
BLAST
Transmembranei558 – 57821HelicalSequence analysisAdd
BLAST
Topological domaini579 – 59517Mitochondrial matrix1 PublicationAdd
BLAST
Transmembranei596 – 61621HelicalSequence analysisAdd
BLAST
Transmembranei622 – 64221HelicalSequence analysisAdd
BLAST
Transmembranei646 – 66621HelicalSequence analysisAdd
BLAST
Transmembranei672 – 69120HelicalSequence analysisAdd
BLAST
Transmembranei702 – 72221HelicalSequence analysisAdd
BLAST
Topological domaini723 – 73917Cytoplasmic1 PublicationAdd
BLAST
Transmembranei740 – 76021HelicalSequence analysisAdd
BLAST
Transmembranei778 – 79720HelicalSequence analysisAdd
BLAST
Transmembranei801 – 81919HelicalSequence analysisAdd
BLAST
Transmembranei833 – 85321HelicalSequence analysisAdd
BLAST
Transmembranei857 – 87923HelicalSequence analysisAdd
BLAST
Topological domaini880 – 1086207Mitochondrial matrix1 PublicationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343Mitochondrion1 PublicationAdd
BLAST
Chaini44 – 10861043NAD(P) transhydrogenase, mitochondrialPRO_0000001054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysineBy similarity
Modified residuei117 – 1171N6-succinyllysineBy similarity
Modified residuei224 – 2241N6-succinyllysineBy similarity
Modified residuei294 – 2941N6-succinyllysineBy similarity
Modified residuei331 – 3311N6-succinyllysineBy similarity
Modified residuei397 – 3971N6-acetyllysineBy similarity
Modified residuei1079 – 10791N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP11024.
PeptideAtlasiP11024.
PRIDEiP11024.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015769.

Structurei

Secondary structure

1
1086
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi914 – 92310Combined sources
Beta strandi925 – 9317Combined sources
Helixi933 – 9375Combined sources
Turni938 – 9403Combined sources
Helixi941 – 95313Combined sources
Beta strandi957 – 9626Combined sources
Beta strandi967 – 9693Combined sources
Helixi972 – 9809Combined sources
Helixi984 – 9863Combined sources
Beta strandi987 – 9893Combined sources
Helixi990 – 9934Combined sources
Helixi994 – 9996Combined sources
Beta strandi1001 – 10077Combined sources
Helixi1010 – 10123Combined sources
Helixi1015 – 10184Combined sources
Turni1023 – 10264Combined sources
Helixi1032 – 10343Combined sources
Beta strandi1038 – 10458Combined sources
Helixi1055 – 10584Combined sources
Beta strandi1062 – 10676Combined sources
Helixi1069 – 108113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D4OX-ray1.21A903-1086[»]
ProteinModelPortaliP11024.
SMRiP11024. Positions 58-441, 907-1083.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11024.

Family & Domainsi

Sequence similaritiesi

In the N-terminal section; belongs to the AlaDH/PNT family.Curated
In the C-terminal section; belongs to the PNT beta subunit family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEMU. Eukaryota.
COG1282. LUCA.
COG3288. LUCA.
GeneTreeiENSGT00390000004624.
HOGENOMiHOG000160623.
HOVERGENiHBG006511.
InParanoidiP11024.
KOiK00323.
OMAiKPGIPYK.
OrthoDBiEOG722J7T.
TreeFamiTF300636.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
InterProiIPR008143. Ala_DH/PNT_CS2.
IPR008142. AlaDH/PNT_CS1.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR016040. NAD(P)-bd_dom.
IPR012136. NADH_DH_b.
IPR026255. NADP_transhyd_a.
IPR024605. NADP_transhyd_a_C.
IPR030168. NADP_transhyd_mt.
[Graphical view]
PANTHERiPTHR10160:SF22. PTHR10160:SF22. 1 hit.
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
PF02233. PNTB. 1 hit.
PF12769. PNTB_4TM. 1 hit.
[Graphical view]
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52467. SSF52467. 1 hit.
TIGRFAMsiTIGR00561. pntA. 1 hit.
PROSITEiPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANLLKTVVT GCSCPFLSNL GSCKVLPGKK NFLRTFHTHR ILWCSAPVKP
60 70 80 90 100
GIPYKQLTVG VPKEIFQNEK RVALSPAGVQ ALVKQGFNVV VESGAGEASK
110 120 130 140 150
FSDDHYRAAG AQIQGAKEVL ASDLVVKVRA PMLNPTLGVH EADLLKTSGT
160 170 180 190 200
LISFIYPAQN PDLLNKLSKR KTTVLAMDQV PRVTIAQGYD ALSSMANIAG
210 220 230 240 250
YKAVVLAANH FGRFFTGQIT AAGKVPPAKI LIVGGGVAGL ASAGAAKSMG
260 270 280 290 300
AIVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE
310 320 330 340 350
MKLFAQQCKE VDILISTALI PGKKAPILFN KEMIESMKEG SVVVDLAAEA
360 370 380 390 400
GGNFETTKPG ELYVHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS
410 420 430 440 450
PDKDNFYFEV KDDFDFGTMG HVIRGTVVMK DGQVIFPAPT PKNIPQGAPV
460 470 480 490 500
KQKTVAELEA EKAATITPFR KTMTSASVYT AGLTGILGLG IAAPNLAFSQ
510 520 530 540 550
MVTTFGLAGI VGYHTVWGVT PALHSPLMSV TNAISGLTAV GGLVLMGGHL
560 570 580 590 600
YPSTTSQGLA ALATFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL
610 620 630 640 650
PAGTFVGGYL ASLYSGYNIE QIMYLGSGLC CVGALAGLST QGTARLGNAL
660 670 680 690 700
GMIGVAGGLA ATLGGLKPCP ELLAQMSGAM ALGGTIGLTI AKRIQISDLP
710 720 730 740 750
QLVAAFHSLV GLAAVLTCIA EYIIEYPHFA TDAAANLTKI VAYLGTYIGG
760 770 780 790 800
VTFSGSLVAY GKLQGILKSA PLLLPGRHLL NAGLLAGSVG GIIPFMMDPS
810 820 830 840 850
FTTGITCLGS VSALSAVMGV TLTAAIGGAD MPVVITVLNS YSGWALCAEG
860 870 880 890 900
FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG
910 920 930 940 950
KPMEISGTHT EINLDNAIDM IREANSIIIT PGYGLCAAKA QYPIADLVKM
960 970 980 990 1000
LSEQGKKVRF GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINHDFPDT
1010 1020 1030 1040 1050
DLVLVIGAND TVNSAAQEDP NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA
1060 1070 1080
AVDNPIFYKP NTAMLLGDAK KTCDALQAKV RESYQK
Length:1,086
Mass (Da):113,854
Last modified:March 18, 2008 - v3
Checksum:iE3663B533B8E7E35
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC114660 mRNA. Translation: AAI14661.1.
J03534 mRNA. Translation: AAA30660.1.
M22754 mRNA. Translation: AAA30717.1.
L02543 mRNA. Translation: AAA21440.1.
PIRiA31670. DEBOXM.
RefSeqiNP_776368.1. NM_173943.3.
XP_005221585.1. XM_005221528.3.
XP_005221586.1. XM_005221529.3.
XP_005221587.1. XM_005221530.3.
UniGeneiBt.5120.

Genome annotation databases

EnsembliENSBTAT00000015769; ENSBTAP00000015769; ENSBTAG00000011885.
GeneIDi280878.
KEGGibta:280878.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC114660 mRNA. Translation: AAI14661.1.
J03534 mRNA. Translation: AAA30660.1.
M22754 mRNA. Translation: AAA30717.1.
L02543 mRNA. Translation: AAA21440.1.
PIRiA31670. DEBOXM.
RefSeqiNP_776368.1. NM_173943.3.
XP_005221585.1. XM_005221528.3.
XP_005221586.1. XM_005221529.3.
XP_005221587.1. XM_005221530.3.
UniGeneiBt.5120.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D4OX-ray1.21A903-1086[»]
ProteinModelPortaliP11024.
SMRiP11024. Positions 58-441, 907-1083.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015769.

Protein family/group databases

TCDBi3.D.2.3.1. the proton-translocating transhydrogenase (pth) family.

Proteomic databases

PaxDbiP11024.
PeptideAtlasiP11024.
PRIDEiP11024.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000015769; ENSBTAP00000015769; ENSBTAG00000011885.
GeneIDi280878.
KEGGibta:280878.

Organism-specific databases

CTDi23530.

Phylogenomic databases

eggNOGiENOG410IEMU. Eukaryota.
COG1282. LUCA.
COG3288. LUCA.
GeneTreeiENSGT00390000004624.
HOGENOMiHOG000160623.
HOVERGENiHBG006511.
InParanoidiP11024.
KOiK00323.
OMAiKPGIPYK.
OrthoDBiEOG722J7T.
TreeFamiTF300636.

Enzyme and pathway databases

ReactomeiR-BTA-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

EvolutionaryTraceiP11024.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
InterProiIPR008143. Ala_DH/PNT_CS2.
IPR008142. AlaDH/PNT_CS1.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR016040. NAD(P)-bd_dom.
IPR012136. NADH_DH_b.
IPR026255. NADP_transhyd_a.
IPR024605. NADP_transhyd_a_C.
IPR030168. NADP_transhyd_mt.
[Graphical view]
PANTHERiPTHR10160:SF22. PTHR10160:SF22. 1 hit.
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
PF02233. PNTB. 1 hit.
PF12769. PNTB_4TM. 1 hit.
[Graphical view]
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52467. SSF52467. 1 hit.
TIGRFAMsiTIGR00561. pntA. 1 hit.
PROSITEiPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Uterus.
  2. "Amino acid sequence of the signal peptide of mitochondrial nicotinamide nucleotide transhydrogenase as determined from the sequence of its messenger RNA."
    Yamaguchi M., Hatefi Y., Trach K., Hoch J.A.
    Biochem. Biophys. Res. Commun. 157:24-29(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-75.
  3. "The primary structure of the mitochondrial energy-linked nicotinamide nucleotide transhydrogenase deduced from the sequence of cDNA clones."
    Yamaguchi M., Hatefi Y., Trach K., Hoch J.A.
    J. Biol. Chem. 263:2761-2767(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-1086, PROTEIN SEQUENCE OF 44-58.
  4. "Characterization of the substrate-binding sites of the mitochondrial nicotinamide nucleotide transhydrogenase."
    Wakabayashi S., Hatefi Y.
    Biochem. Int. 15:915-924(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 280-290 AND 1044-1049.
  5. "Amino acid sequence of the NAD (H)-binding region of the mitochondrial nicotinamide nucleotide transhydrogenase modified by N,N'-dicyclohexylcarbodiimide."
    Wakabayashi S., Hatefi Y.
    Biochem. Int. 15:667-675(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 291-302.
  6. "Mitochondrial energy-linked nicotinamide nucleotide transhydrogenase. Membrane topography of the bovine enzyme."
    Yamaguchi M., Hatefi Y.
    J. Biol. Chem. 266:5728-5735(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  7. "Crystal structure of transhydrogenase domain III at 1.2 A resolution."
    Prasad G.S., Sridhar V., Yamaguchi M., Hatefi Y., Stout C.D.
    Nat. Struct. Biol. 6:1126-1131(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 903-1086.

Entry informationi

Entry nameiNNTM_BOVIN
AccessioniPrimary (citable) accession number: P11024
Secondary accession number(s): A4FUB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 18, 2008
Last modified: July 6, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.