ID M9MHX6_PSEA3 Unreviewed; 1584 AA.
AC M9MHX6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=PANT_22d00047 {ECO:0000313|EMBL:GAC76477.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC76477.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 6/6.
CC {ECO:0000256|ARBA:ARBA00005145}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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DR EMBL; DF196788; GAC76477.1; -; Genomic_DNA.
DR STRING; 1151754.M9MHX6; -.
DR OrthoDB; 68574at2759; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR CDD; cd06224; REM; 1.
DR CDD; cd11883; SH3_Sdc25; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR006255; SucB.
DR NCBIfam; TIGR01347; sucB; 1.
DR PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00229; RasGEFN; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Guanine-nucleotide releasing factor {ECO:0000256|PROSITE-ProRule:PRU00135};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 30..89
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 854..987
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 1174..1250
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1584 AA; 170186 MW; E31CA8A5370F22F9 CRC64;
MSSWASASSS QAQASFTPAL SDNEDELDIQ PEEHVVALHD FNSNNATCLS FQAGQVIRVY
NRDPSGWWDG ELDGQRGWFP SNYVDQEAVY VSDDGHGNSS FSYHHPDLLR PASISRASSH
HHTPSAPADT PHHQRYFSAT SSRSSTPTST PLVDRGDAGV LDPILHAISL LRNAVRANRV
AHFQPSTACV ISSVRSVLSA TDCLTRESPV LKANPQLARE RKAILSELSK LVAQARTASA
PMVDETQRPR EMDSMLQLAD HVLANVRDFL TVALESGVPV PDRRSSVYDD LYTSRTADAA
AAAAPPADPG TRPANPPHEL DKTPTPQYPN ARASASASAP GYPSRQEYAA TYDTATGYTD
TRRSYLQHRH PSDGSLESSE EGAHAIAQAR SITQRQLNGR AETVAAAVAN HLGMARSRSD
SSSESPDSTS GHDTGSHHGS AGSADDDEPP APIERTPYEV MQRLSITNDQ LLSIIAAFIG
HVHTHTSESH ASSYAHLIDM TREAVVGVRN LLLVVEAVNN NVVLQQLRPR QTSILWETRE
NLYEATTQLV TAARIVTSAP SASITAGSAA EAEDKSRLLQ AATSVLRTGG ECVGAVRLCV
DRLEPGFTIS LPEPSRSRHP RASSQSRASA EPESNGHSGE HGDARTGDAR TDDADADAAR
ETRRKNTLSF LGRKATSLSS LKQKYERGEH STDFEDIDED DHSGEESEAS KPGGRTAHAM
SSRSSSLMGA APSSGDRTSH PAQARTSVPG SSASGVGSSV EMLSEDAART SRSTIQSIRS
ECTGETSARP SLEAQLATAT VPDAHTTAQT AAKQLAGGVV DRQSMYREHR GPTSSLEARY
MAPDYDPSDV VCNSEGQVTG ATLKALVEKM TPHDTMVEAT FSSSFFLCFR MFSSPQELLD
ALVARFEMRP PADVPMSEAD VARWNDKKLV PVRLRVLNLI KNWLENHWNP VTDRVILQQL
IPFAERCTSA GGGAGKAGWR SVSAGEGPGS GKIRAVRPAV FSAWLYTRWE RTAKGVGQGA
ASVLTEPAAR RHGQAAHSRA RAHRQILRSS PALGLGVDRC GQVWTVSTKP RDHRSSAPQH
PFISIASSLP SRIDESPFLS ILSAPIMFPR SIAQSGARAA RSLALRSGSV RMVTPAVARR
TLITATAQKS LAIAAHNMTT LPAQRNFSSS ASRKEIVKVP QMAESITEGT LKQWNKKVGD
FVQADEEVAT IETDKVRASS ARAPLSGTIV EVFANEEDTV EVGKDLFKLE PGEAPAGGAK
KEEKTEEKKE DKKEDKPKKE ESKQQQQPEK KGDDKKPAPA AEPESRPSAA NSTPPPSKPS
SSSSSPSSKS SPSSGSSSSS SSAPKPAAGS REENRVKMSR MRLRIAERLK QSQNTAASLT
TFNEIDMSNL MAFRARHKDR ILKEKGVKLG FMSAFAKASA MALKDVPAAN ASIEGAGLGD
TIVYRDYVDL SVAVSTDKGL VTPVVRNLEG MSLIEIEEAI AGLGKKARDN KLTLEDMSGG
TFTISNGGVF GSLFGTPILN LPGSAILGMH AVKDKAWVVN GKVEIRPIMV VALTYDHRLL
DGREAVTFLV KLKQYIEDMP SMLL
//
