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Database: UniProt/TrEMBL
Entry: Q3M8A2_ANAVT
LinkDB: Q3M8A2_ANAVT
Original site: Q3M8A2_ANAVT 
ID   Q3M8A2_ANAVT            Unreviewed;       432 AA.
AC   Q3M8A2;
DT   25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2005, sequence version 1.
DT   28-MAR-2018, entry version 89.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=Ava_3176 {ECO:0000313|EMBL:ABA22784.1};
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292 {ECO:0000313|EMBL:ABA22784.1, ECO:0000313|Proteomes:UP000002533};
RN   [1] {ECO:0000313|Proteomes:UP000002533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937 {ECO:0000313|Proteomes:UP000002533};
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S.,
RA   Han C., Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; CP000117; ABA22784.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q3M8A2; -.
DR   STRING; 240292.Ava_3176; -.
DR   EnsemblBacteria; ABA22784; ABA22784; Ava_3176.
DR   KEGG; ava:Ava_3176; -.
DR   eggNOG; ENOG4107UKP; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H04EL; -.
DR   BioCyc; AVAR240292:G7WH-7517-MONOMER; -.
DR   Proteomes; UP000002533; Chromosome.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 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   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 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   ECO:0000313|EMBL:ABA22784.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002533};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ABA22784.1}.
FT   DOMAIN        3     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      131    168       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   432 AA;  44963 MW;  1AD69F6E1B9D16D9 CRC64;
     MSIHEIFMPA LSSTMTEGKI VSWVKSPGDK VEKGETVVVV ESDKADMDVE TFYEGYLAHI
     IVEAGDSAPV GAAIAYVAET EAEIEAAKSL GSSGGAAATP SAPPEPVAAT AAVGVPAASQ
     NGSNHREGRL VASPRARKLA KELKVDLTSL KGSGPYGRIV ADDIEAAVGK VKQPATTPTA
     PTPTFTPAPV PATRTPAPAP APAPVAAAPG QVVPFNTLQN AVIRNMVASL DVPVFRVGYT
     ITTDGLDKLY KQIKSKGVTM TALLAKAVAV TLQKHPLLNA SYSDQGLVYH PDINIAVAVA
     MDGGGLITPV LKNADKIDIY SLSRTWKSLV DKARSKQLQP DEYSGGNFTL SNLGMFGVDT
     FDAILPPGQG SILAIGASRP QLVATGDGSF AIKQQMQVNI TSDHRIIYGA DAAAFLQDLA
     KLIETDAQSL TL
//
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