ID H2ATB3_KAZAF Unreviewed; 412 AA.
AC H2ATB3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE RecName: Full=Lipoyl-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=KAFR0C06210 {ECO:0000313|EMBL:CCF57613.1};
GN ORFNames=KAFR_0C06210 {ECO:0000313|EMBL:CCF57613.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF57613.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF57613.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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DR EMBL; HE650823; CCF57613.1; -; Genomic_DNA.
DR RefSeq; XP_003956748.1; XM_003956699.1.
DR AlphaFoldDB; H2ATB3; -.
DR STRING; 1071382.H2ATB3; -.
DR GeneID; 13885531; -.
DR KEGG; kaf:KAFR_0C06210; -.
DR eggNOG; KOG0557; Eukaryota.
DR HOGENOM; CLU_035825_2_1_1; -.
DR InParanoid; H2ATB3; -.
DR OrthoDB; 52212at2759; -.
DR Proteomes; UP000005220; Chromosome 3.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF82; PYRUVATE DEHYDROGENASE COMPLEX PROTEIN X COMPONENT, MITOCHONDRIAL; 1.
DR Pfam; PF00364; Biotin_lipoyl; 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 Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 32..108
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 169..210
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 125..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 46225 MW; 1A26FCBAA09ABEC5 CRC64;
MLGINLVRTA ARLVLKRNSA RCLHNSAKVW DIQPFLMPAM SPTMEKGGIV SWKVEVGNTF
SAGDVLLEVE TDKAQIDVEA QDDGKLAKIL RKDGSKDISV GETIAFIAEP NDDLSTLEIP
EIAQDKREKA HASSGKKDEL QAKSSPQATP TKGAKRSAVK LHTANPNQTL LPSVSLLLAE
NNLSKEDAFN NIEATGLNGR LLKGDVLAYL GRIDNENLLG ITEYIRNSES LDLSNIKVKP
RQAMETQEIS KEKVEETKKE AAIKKAPLIL NEEIILTVPS EVNELKLSKS LRSFIDEAYH
YTHRASLENE QSNYFDAIFD ELTTPNLRAP RFKYSYDIIP LNTNSNNMMG EEDDIFDILS
SRKRRASVES RRNNEKTNDY LLNLRVAVSN RFLDSEKKAS RFIEYIKQVE IF
//