NAD(P) transhydrogenase, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot P11024 (NNTM_BOVIN)

Last modified November 25, 2008. Version 87. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    NAD(P) transhydrogenase, mitochondrial
    EC=1.6.1.2
Alternative name(s):
    Nicotinamide nucleotide transhydrogenase
    Pyridine nucleotide transhydrogenase

Gene names

Name:

NNT

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	1086 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.
Catalytic activity	NADPH + NAD(+) = NADP(+) + NADH.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein; Matrix sidePotential.
Sequence similarities	In the N-terminal section; belongs to the AlaDH/PNT family. In the C-terminal section; belongs to the PNT beta subunit family.

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Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD(P)+ transhydrogenase (AB-specific) activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 43

Mitochondrion

Chain

44 – 1086

1043

NAD(P) transhydrogenase, mitochondrial

PRO_0000001054

Regions

Topological domain

44 – 474

431

Mitochondrial matrix

Transmembrane

475 – 493

Potential

Transmembrane

501 – 521

Potential

Transmembrane

527 – 546

Potential

Transmembrane

558 – 578

Potential

Topological domain

579 – 595

Mitochondrial matrix

Transmembrane

596 – 616

Potential

Transmembrane

622 – 642

Potential

Transmembrane

646 – 666

Potential

Transmembrane

672 – 691

Potential

Transmembrane

702 – 722

Potential

Topological domain

723 – 739

Cytoplasmic

Transmembrane

740 – 760

Potential

Transmembrane

778 – 797

Potential

Transmembrane

801 – 819

Potential

Transmembrane

833 – 853

Potential

Transmembrane

857 – 879

Potential

Topological domain

880 – 1086

207

Mitochondrial matrix

Nucleotide binding

229 – 259

NAD By similarity

Secondary structure

1086

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P11024-1 [UniParc].

Last modified March 18, 2008. Version 3.
Checksum: E3663B533B8E7E35
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FASTA

1,086

113,854

        10         20         30         40         50         60 
MANLLKTVVT GCSCPFLSNL GSCKVLPGKK NFLRTFHTHR ILWCSAPVKP GIPYKQLTVG 

        70         80         90        100        110        120 
VPKEIFQNEK RVALSPAGVQ ALVKQGFNVV VESGAGEASK FSDDHYRAAG AQIQGAKEVL 

       130        140        150        160        170        180 
ASDLVVKVRA PMLNPTLGVH EADLLKTSGT LISFIYPAQN PDLLNKLSKR KTTVLAMDQV 

       190        200        210        220        230        240 
PRVTIAQGYD ALSSMANIAG YKAVVLAANH FGRFFTGQIT AAGKVPPAKI LIVGGGVAGL 

       250        260        270        280        290        300 
ASAGAAKSMG AIVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE 

       310        320        330        340        350        360 
MKLFAQQCKE VDILISTALI PGKKAPILFN KEMIESMKEG SVVVDLAAEA GGNFETTKPG 

       370        380        390        400        410        420 
ELYVHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS PDKDNFYFEV KDDFDFGTMG 

       430        440        450        460        470        480 
HVIRGTVVMK DGQVIFPAPT PKNIPQGAPV KQKTVAELEA EKAATITPFR KTMTSASVYT 

       490        500        510        520        530        540 
AGLTGILGLG IAAPNLAFSQ MVTTFGLAGI VGYHTVWGVT PALHSPLMSV TNAISGLTAV 

       550        560        570        580        590        600 
GGLVLMGGHL YPSTTSQGLA ALATFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL 

       610        620        630        640        650        660 
PAGTFVGGYL ASLYSGYNIE QIMYLGSGLC CVGALAGLST QGTARLGNAL GMIGVAGGLA 

       670        680        690        700        710        720 
ATLGGLKPCP ELLAQMSGAM ALGGTIGLTI AKRIQISDLP QLVAAFHSLV GLAAVLTCIA 

       730        740        750        760        770        780 
EYIIEYPHFA TDAAANLTKI VAYLGTYIGG VTFSGSLVAY GKLQGILKSA PLLLPGRHLL 

       790        800        810        820        830        840 
NAGLLAGSVG GIIPFMMDPS FTTGITCLGS VSALSAVMGV TLTAAIGGAD MPVVITVLNS 

       850        860        870        880        890        900 
YSGWALCAEG FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG 

       910        920        930        940        950        960 
KPMEISGTHT EINLDNAIDM IREANSIIIT PGYGLCAAKA QYPIADLVKM LSEQGKKVRF 

       970        980        990       1000       1010       1020 
GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINHDFPDT DLVLVIGAND TVNSAAQEDP 

      1030       1040       1050       1060       1070       1080 
NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA AVDNPIFYKP NTAMLLGDAK KTCDALQAKV 


RESYQK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3196335] [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: 3277960] [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: 3325062] [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: 3426633] [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: 2005110] [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: 10581554] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 903-1086.

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Cross-references

Sequence databases

BC114660 mRNA. Translation: AAI14661.1.
J03534 mRNA. Translation: AAA30660.1.
M22754 mRNA. Translation: AAA30717.1.
L02543 mRNA. Translation: AAA21440.1.

PIR

DEBOXM. A31670.

RefSeq

NP_776368.1.

UniGene

Bt.5120

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D4O	X-ray	1.21	A	903-1086	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSBTAG00000011885. Bos taurus. [Contig view]

GeneID

280878.

KEGG

bta:280878.

Phylogenomic databases

HOVERGEN

P11024.

Family and domain databases

InterPro

IPR007698. Ala_DHase/PNT_C.
IPR008142. Ala_DHase/PNT_CS1.
IPR008143. Ala_DHase/PNT_CS2.
IPR007886. Ala_DHase/PNT_N.
IPR016040. NAD(P)-bd.
IPR004571. NADP_transhyd_a.
IPR004003. NADP_transhyd_b.
[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.
PF02233. PNTB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00561. pntA. 1 hit.

PROSITE

PS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

NNTM_BOVIN

Accession

Primary (citable) accession number: P11024
Secondary accession number(s): A4FUB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	March 18, 2008
Last modified:	November 25, 2008
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents