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Database: UniProt
Entry: F0FTH4_STRSA
LinkDB: F0FTH4_STRSA
Original site: F0FTH4_STRSA 
ID   F0FTH4_STRSA            Unreviewed;       419 AA.
AC   F0FTH4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   Name=acoC {ECO:0000313|EMBL:EGC26350.1};
GN   ORFNames=HMPREF9392_1253 {ECO:0000313|EMBL:EGC26350.1};
OS   Streptococcus sanguinis SK678.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=888819 {ECO:0000313|EMBL:EGC26350.1, ECO:0000313|Proteomes:UP000003133};
RN   [1] {ECO:0000313|EMBL:EGC26350.1, ECO:0000313|Proteomes:UP000003133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK678 {ECO:0000313|EMBL:EGC26350.1,
RC   ECO:0000313|Proteomes:UP000003133};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGC26350.1}.
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DR   EMBL; AEXA01000006; EGC26350.1; -; Genomic_DNA.
DR   RefSeq; WP_002900385.1; NZ_GL872319.1.
DR   AlphaFoldDB; F0FTH4; -.
DR   GeneID; 61536420; -.
DR   PATRIC; fig|888819.3.peg.1232; -.
DR   HOGENOM; CLU_016733_10_2_9; -.
DR   Proteomes; UP000003133; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EGC26350.1}.
FT   DOMAIN          2..80
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          130..167
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          88..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  44583 MW;  70098CEB49B6A438 CRC64;
     MATEIVMPKL GLTMTEGLIN NWLVKEGDTV AAGQPVLEIS SEKLTSDVEA PSAGVILKII
     SQAGDTVPCK KVIAWIGEAG ESILGMEAGG ASANQSESEQ EAADAEPELA EKTATASSNS
     VGNSEHGRIF ITPLARKIAK EKGYDISLIS GTGGNGRITR RDVENYKPEA LPNQTPESSS
     AVLQHAGQVD YGAGLTGMRK TIAERMMNSL QASAQVTLHR KVDISRLIAF RQDMKDKVAS
     PLENGEISIT TLLTKAVAKA LKDHPQLNAW YFNGQYQEVE DIHIGIATAL SDGLVVPVIR
     HVDKLTLADL GLAIKTEANQ ARKGTLDPAL YSGSTFSITN LGGAGIEYFT PILNTPEVAI
     LGVGALQTSL ALDSQGQVYE QKFLPLSLTF DHQVVDGQPA AEFLASLADK LESPYDLVF
//
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