(data stored in ACNUC5340 zone)

HOGENOM: AEDAE_3502_PE8

ID   AEDAE_3502_PE8                       STANDARD;      PRT;   232 AA.
AC   AEDAE_3502_PE8; Q0IEK7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Putative lipoyltransferase 2, mitochondrial; EC=2.3.1 181;
DE   (AEDAE_3502.PE8).
GN   ORFNames=AAEL009657, AaeL_AAEL009657;
OS   AEDES AEGYPTI.
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera;
OC   Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; Culicinae;
OC   Culicini; Aedes.
OX   NCBI_TaxID=7159;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AEDAE_3502.PE8.
CC       Aedes aegypti supercontig supercont1.415 AaegL1  sequence 1..1112054
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:Q0IEK7_AEDAE
CC   -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic
CC       acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of
CC       lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate
CC       although octanoyl-ACP is likely to be the physiological substrate
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Octanoyl-[acyl-carrier-protein] + protein =
CC       protein N(6)-(octanoyl)lysine + [acyl-carrier-protein].
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the lipB family.
CC   -!- GENE_FAMILY: HOG000194322 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Aedes_aegypti;AAEL009657;AAEL009657-RA;AAEL009657-PA.
DR   EMBL; CH477600; - ;
DR   UniProtKB/Swiss-Prot; Q0IEK7; -.
DR   EMBL; CH477600; EAT38456.1; -; Genomic_DNA.
DR   RefSeq; XP_001653907.1; XM_001653857.1.
DR   UniGene; Aae.8785; -.
DR   ProteinModelPortal; Q0IEK7; -.
DR   STRING; Q0IEK7; -.
DR   EnsemblMetazoa; AAEL009657-RA; AAEL009657-PA; AAEL009657.
DR   GeneID; 5580024; -.
DR   KEGG; aag:AaeL_AAEL009657; -.
DR   VectorBase; AAEL009657; Aedes aegypti.
DR   eggNOG; inNOG05477; -.
DR   GeneTree; EMGT00050000017016; -.
DR   OMA; MRQPAVR; -.
DR   OrthoDB; EOG4JDFPV; -.
DR   PhylomeDB; Q0IEK7; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:EC.
DR   GO; GO:0016415; F:octanoyltransferase activity; IEA:InterPro.
DR   GO; GO:0009107; P:lipoate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   HAMAP; MF_00013; LipB; 1; -.
DR   InterPro; IPR004143; BPL_LipA_LipB.
DR   InterPro; IPR000544; Octanoyltransferase.
DR   InterPro; IPR020605; Octanoyltransferase_CS.
DR   PANTHER; PTHR10993:SF0; PTHR10993:SF0; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   PIRSF; PIRSF016262; LPLase; 1.
DR   TIGRFAMs; TIGR00214; LipB; 1.
DR   PROSITE; PS01313; LIPB; 1.
DR   HOGENOMDNA; AEDAE_3502.PE8; -.
KW   AAEL0096573; AAEL009657-PA ; Q0IEK7; CH477600;
KW   Acyltransferase; Complete proteome; Ligase; Mitochondrion;
KW   Reference proteome; Transferase.
SQ   SEQUENCE   232 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSRVVHILRA GKLSYQKSLN LQKAVSSAVL NGDQSNVLIL TEHDPVYTVG IRTKSYGPEE
     ERRLKALGAE FFRTNRGGLI TFHGPGQLVA YPVLNLKNFQ PSVRWYVCHI EKTVIDLCRR
     YGLKAGTTED TGVWIGDRKI CAIGIHASRY VTTHGLALNC NNDLGWFKHI VPCGIEGKGV
     TSLSAELSRE VPVEEATAKF LESFRDVLQC DLKELEPDKQ REILGQGCSF SS
//

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