LIPT2_DANRE
ID LIPT2_DANRE Reviewed; 224 AA.
AC Q29R99;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Putative lipoyltransferase 2, mitochondrial;
DE EC=2.3.1.181;
DE AltName: Full=Lipoate-protein ligase B;
DE AltName: Full=Lipoyl/octanoyl transferase;
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
DE Flags: Precursor;
GN Name=lipt2; ORFNames=zgc:136925;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-
CC dependent enzymes, which catalyze essential redox reactions (By
CC similarity). Lipoyl-ACP can also act as a substrate although octanoyl-
CC ACP is likely to be the physiological substrate (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:A6NK58}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-
CC octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-
CC COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181;
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:A6NK58}.
CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic
CC acid is attached via an amide linkage to the epsilon-amino group of a
CC specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000305}.
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DR EMBL; BC114309; AAI14310.1; -; mRNA.
DR RefSeq; NP_001035082.1; NM_001039993.1.
DR AlphaFoldDB; Q29R99; -.
DR SMR; Q29R99; -.
DR STRING; 7955.ENSDARP00000092768; -.
DR PaxDb; Q29R99; -.
DR GeneID; 664765; -.
DR KEGG; dre:664765; -.
DR CTD; 387787; -.
DR ZFIN; ZDB-GENE-060312-18; lipt2.
DR eggNOG; KOG0325; Eukaryota.
DR InParanoid; Q29R99; -.
DR PhylomeDB; Q29R99; -.
DR Reactome; R-DRE-389661; Glyoxylate metabolism and glycine degradation.
DR UniPathway; UPA00538; UER00592.
DR PRO; PR:Q29R99; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:2000376; P:positive regulation of oxygen metabolic process; ISS:UniProtKB.
DR GO; GO:0009249; P:protein lipoylation; ISS:UniProtKB.
DR CDD; cd16444; LipB; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00013; LipB; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR000544; Octanoyltransferase.
DR InterPro; IPR020605; Octanoyltransferase_CS.
DR PIRSF; PIRSF016262; LPLase; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00214; lipB; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR PROSITE; PS01313; LIPB; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Ligase; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..224
FT /note="Putative lipoyltransferase 2, mitochondrial"
FT /id="PRO_0000332307"
FT DOMAIN 37..217
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 178
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 81..88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147..149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160..162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 144
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000250"
SQ SEQUENCE 224 AA; 24664 MW; E4BC321FABD74E37 CRC64;
MSVTKAAVKA VHLGRISYHS ALKIQQQHIQ QHLDSSSNIP NTLLLCEHEP VYTIGLRQAP
YPPAEEQRLK ALGADFCRTN RGGLITFHGP GQLVCYPILN LGCFKKSVRW YVCELERTVI
KMCGKFGIKA STSPDTGVWV GDNKICAIGI HCGRYITSHG LALNCNTDMS WFDNIVPCGI
VGKGVTSLSQ ELERDVPPDE AIPKLLEAFT EQFNCTLTYN GSLS