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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071Substrate; via amide nitrogen and carbonyl oxygen
Binding sitei151 – 1511Substrate
Binding sitei161 – 1611Substrate
Binding sitei179 – 1791Substrate
Binding sitei208 – 2081Substrate; via amide nitrogen
Binding sitei210 – 2101Substrate; via amide nitrogen

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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionAdd
BLAST
Chaini26 – 373348Lipoyltransferase 1, mitochondrialPRO_0000017855Add
BLAST

Proteomic databases

PaxDbiO46419.
PRIDEiO46419.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005171.

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 376Combined sources
Helixi41 – 5414Combined sources
Beta strandi62 – 665Combined sources
Beta strandi69 – 746Combined sources
Helixi80 – 834Combined sources
Helixi86 – 905Combined sources
Turni91 – 933Combined sources
Beta strandi95 – 984Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi112 – 1198Combined sources
Helixi121 – 1233Combined sources
Helixi126 – 14015Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi154 – 1563Combined sources
Turni157 – 1593Combined sources
Beta strandi160 – 1634Combined sources
Beta strandi165 – 1695Combined sources
Beta strandi174 – 18310Combined sources
Helixi186 – 1927Combined sources
Beta strandi199 – 2024Combined sources
Helixi215 – 2184Combined sources
Helixi224 – 23916Combined sources
Beta strandi246 – 2483Combined sources
Turni253 – 2553Combined sources
Helixi259 – 2679Combined sources
Helixi269 – 2724Combined sources
Turni273 – 2753Combined sources
Beta strandi279 – 28810Combined sources
Beta strandi293 – 30311Combined sources
Beta strandi306 – 3138Combined sources
Turni316 – 3183Combined sources
Helixi321 – 33111Combined sources
Beta strandi334 – 3363Combined sources
Helixi341 – 3499Combined sources
Helixi357 – 37014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5AX-ray2.10A27-373[»]
3A7UX-ray3.44A27-373[»]
ProteinModelPortaliO46419.
SMRiO46419. Positions 31-373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO46419.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 243187BPL/LPL catalyticPROSITE-ProRule annotationAdd
BLAST

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.
OrthoDBiEOG7N37DX.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5AX-ray2.10A27-373[»]
3A7UX-ray3.44A27-373[»]
ProteinModelPortaliO46419.
SMRiO46419. Positions 31-373.
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.
OrthoDBiEOG7N37DX.
TreeFamiTF314085.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiO46419.
NextBioi20806513.

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...

Publicationsi

  1. "Cloning and expression of a cDNA encoding bovine lipoyltransferase."
    Fujiwara K., Okamura-Ikeda K., Motokawa Y.
    J. Biol. Chem. 272:31974-31978(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. "Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP."
    Fujiwara K., Hosaka H., Matsuda M., Okamura-Ikeda K., Motokawa Y., Suzuki M., Nakagawa A., Taniguchi H.
    J. Mol. Biol. 371:222-234(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-373 IN COMPLEX WITH LIPOYL-AMP, FUNCTION.

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: February 17, 2016
This is version 95 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.