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Database: UniProt
Entry: A0A3Q4GIM4_NEOBR
LinkDB: A0A3Q4GIM4_NEOBR
Original site: A0A3Q4GIM4_NEOBR 
ID   A0A3Q4GIM4_NEOBR        Unreviewed;       477 AA.
AC   A0A3Q4GIM4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000008831.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000008831.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR   AlphaFoldDB; A0A3Q4GIM4; -.
DR   STRING; 32507.ENSNBRP00000008831; -.
DR   Ensembl; ENSNBRT00000009087.1; ENSNBRP00000008831.1; ENSNBRG00000006874.1.
DR   GeneTree; ENSGT00940000156750; -.
DR   OMA; TIPHFTY; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000006874; Expressed in skeletal muscle tissue and 6 other cell types or tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:RHEA.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Transferase {ECO:0000256|RuleBase:RU003423};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          45..120
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          155..192
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   477 AA;  51567 MW;  568EC828959A51F2 CRC64;
     MAAVTRGSLG AFRRLLVSKY KLRIVLSLSD NVTVLFCPAV NQGPIVQFKL SDIGEGIMEV
     TVKEWYVKEG DKVSQFDSIC EVQSDKASVT ITSRYDGVIK KLYYDVDATA FVGKPLVDIE
     TESGSEVIQE EDVVETPAMA QEEHTHQEIK GHKTQATPAV RRLAIENNIK LSEVVGTGKD
     GRILKEDILN FLAKQTGAIL PPAPFQEIQT PPPAPAAAPA AAKPVSTKAA VKPPPATPKP
     VFTGKDVTEP LKGVQKAMVK TMTVALKIPH FGYCDEVDLS RLVALRSELK PLAESRGVRL
     SYMPFFIKAA SLGLHHFPIL NASVDEDCQN ITYKASHNIG LAMDTSQGLL VPNVKNVQLL
     SVLEIALELN RLQVLGASGQ LGTADLMGGT FTLSNIGSIG GTYAKPVILP PEVAIGALGK
     IQVLPRFDAA GQVVPAHIMK VSWSADHRII DGATMCRFSN LWREYLENPA SMVLDLK
//
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