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Protein

Lipoyltransferase 1, mitochondrial

Gene

LIPT1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of lipoate-dependent enzymes.1 Publication

Catalytic activityi

Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP.

Pathwayi: protein lipoylation via exogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from lipoate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Lipoyltransferase 1, mitochondrial (LIPT1)
This subpathway is part of the pathway protein lipoylation via exogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from lipoate, the pathway protein lipoylation via exogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei107Substrate; via amide nitrogen and carbonyl oxygen1
Binding sitei151Substrate1
Binding sitei161Substrate1
Binding sitei179Substrate1
Binding sitei208Substrate; via amide nitrogen1
Binding sitei210Substrate; via amide nitrogen1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.181. 908.
ReactomeiR-BTA-389661. Glyoxylate metabolism and glycine degradation.
UniPathwayiUPA00537; UER00595.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyltransferase 1, mitochondrial (EC:2.3.1.-)
Alternative name(s):
Lipoate biosynthesis protein
Lipoate-protein ligase
Lipoyl ligase
Gene namesi
Name:LIPT1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 11

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 25MitochondrionAdd BLAST25
ChainiPRO_000001785526 – 373Lipoyltransferase 1, mitochondrialAdd BLAST348

Proteomic databases

PaxDbiO46419.
PRIDEiO46419.

Expressioni

Gene expression databases

BgeeiENSBTAG00000003965.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005171.

Structurei

Secondary structure

1373
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 37Combined sources6
Helixi41 – 54Combined sources14
Beta strandi62 – 66Combined sources5
Beta strandi69 – 74Combined sources6
Helixi80 – 83Combined sources4
Helixi86 – 90Combined sources5
Turni91 – 93Combined sources3
Beta strandi95 – 98Combined sources4
Beta strandi106 – 108Combined sources3
Beta strandi112 – 119Combined sources8
Helixi121 – 123Combined sources3
Helixi126 – 140Combined sources15
Beta strandi141 – 143Combined sources3
Beta strandi146 – 148Combined sources3
Beta strandi150 – 152Combined sources3
Beta strandi154 – 156Combined sources3
Turni157 – 159Combined sources3
Beta strandi160 – 163Combined sources4
Beta strandi165 – 169Combined sources5
Beta strandi174 – 183Combined sources10
Helixi186 – 192Combined sources7
Beta strandi199 – 202Combined sources4
Helixi215 – 218Combined sources4
Helixi224 – 239Combined sources16
Beta strandi246 – 248Combined sources3
Turni253 – 255Combined sources3
Helixi259 – 267Combined sources9
Helixi269 – 272Combined sources4
Turni273 – 275Combined sources3
Beta strandi279 – 288Combined sources10
Beta strandi293 – 303Combined sources11
Beta strandi306 – 313Combined sources8
Turni316 – 318Combined sources3
Helixi321 – 331Combined sources11
Beta strandi334 – 336Combined sources3
Helixi341 – 349Combined sources9
Helixi357 – 370Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E5AX-ray2.10A27-373[»]
3A7UX-ray3.44A27-373[»]
ProteinModelPortaliO46419.
SMRiO46419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO46419.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini57 – 243BPL/LPL catalyticPROSITE-ProRule annotationAdd BLAST187

Sequence similaritiesi

Belongs to the LplA family.Curated
Contains 1 BPL/LPL catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3159. Eukaryota.
COG0095. LUCA.
GeneTreeiENSGT00390000008846.
HOGENOMiHOG000260595.
HOVERGENiHBG028203.
InParanoidiO46419.
KOiK10105.
OMAiWRNAETV.
OrthoDBiEOG091G09SS.
TreeFamiTF314085.

Family and domain databases

InterProiIPR004143. BPL_LPL_catalytic.
IPR004562. LipoylTrfase_LipoateP_Ligase.
[Graphical view]
TIGRFAMsiTIGR00545. lipoyltrans. 1 hit.
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O46419-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIPFSMKNC FQLLCNLKVP AAGFKNTVKS GLILQSISND VYHNLAVEDW
60 70 80 90 100
IHDHMNLEGK PVLFLWRNSP TVVIGRHQNP WQECNLNLMR EEGVKLARRR
110 120 130 140 150
SGGGTVYHDM GNINLTFFTT KKKYDRMENL KLVVRALKAV HPHLDVQATK
160 170 180 190 200
RFDLLLDGQF KISGTASKIG RNAAYHHCTL LCGTDGTFLS SLLKSPYQGI
210 220 230 240 250
RSNATASTPA LVKNLMEKDP TLTCEVVINA VATEYATSHQ IDNHIHLINP
260 270 280 290 300
TDETVFPGIN SKAIELQTWE WIYGKTPKFS VDTSFTVLHE QSHVEIKVFI
310 320 330 340 350
DVKNGRIEVC NIEAPDHWLP LEICDQLNSS LIGSKFSPIE TTVLTSILHR
360 370
TYPGDDELHS KWNILCEKIK GIM
Length:373
Mass (Da):42,072
Last modified:June 1, 1998 - v1
Checksum:i101ECE836B9D11E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006441 mRNA. Translation: BAA24354.1.
RefSeqiNP_777220.1. NM_174795.2.
UniGeneiBt.4519.

Genome annotation databases

EnsembliENSBTAT00000005171; ENSBTAP00000005171; ENSBTAG00000003965.
GeneIDi286864.
KEGGibta:286864.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006441 mRNA. Translation: BAA24354.1.
RefSeqiNP_777220.1. NM_174795.2.
UniGeneiBt.4519.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E5AX-ray2.10A27-373[»]
3A7UX-ray3.44A27-373[»]
ProteinModelPortaliO46419.
SMRiO46419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005171.

Proteomic databases

PaxDbiO46419.
PRIDEiO46419.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000005171; ENSBTAP00000005171; ENSBTAG00000003965.
GeneIDi286864.
KEGGibta:286864.

Organism-specific databases

CTDi51601.

Phylogenomic databases

eggNOGiKOG3159. Eukaryota.
COG0095. LUCA.
GeneTreeiENSGT00390000008846.
HOGENOMiHOG000260595.
HOVERGENiHBG028203.
InParanoidiO46419.
KOiK10105.
OMAiWRNAETV.
OrthoDBiEOG091G09SS.
TreeFamiTF314085.

Enzyme and pathway databases

UniPathwayiUPA00537; UER00595.
BRENDAi2.3.1.181. 908.
ReactomeiR-BTA-389661. Glyoxylate metabolism and glycine degradation.

Miscellaneous databases

EvolutionaryTraceiO46419.

Gene expression databases

BgeeiENSBTAG00000003965.

Family and domain databases

InterProiIPR004143. BPL_LPL_catalytic.
IPR004562. LipoylTrfase_LipoateP_Ligase.
[Graphical view]
TIGRFAMsiTIGR00545. lipoyltrans. 1 hit.
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIPT_BOVIN
AccessioniPrimary (citable) accession number: O46419
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 1998
Last modified: November 30, 2016
This is version 100 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.