ID D0SUN5_ACILW Unreviewed; 404 AA.
AC D0SUN5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|ARBA:ARBA00019511, ECO:0000256|RuleBase:RU361138};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945, ECO:0000256|RuleBase:RU361138};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|RuleBase:RU361138};
GN Name=sucB {ECO:0000313|EMBL:EEY90590.1};
GN ORFNames=HMPREF0017_01009 {ECO:0000313|EMBL:EEY90590.1};
OS Acinetobacter lwoffii SH145.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575588 {ECO:0000313|EMBL:EEY90590.1, ECO:0000313|Proteomes:UP000018425};
RN [1] {ECO:0000313|Proteomes:UP000018425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH145 {ECO:0000313|Proteomes:UP000018425};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
CC -!- FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the second step in the conversion of 2-
CC oxoglutarate to succinyl-CoA and CO(2). {ECO:0000256|ARBA:ARBA00004052,
CC ECO:0000256|RuleBase:RU361138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000256|ARBA:ARBA00001267,
CC ECO:0000256|RuleBase:RU361138};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU361138};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000256|RuleBase:RU361138};
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, ECO:0000256|RuleBase:RU361138}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361138}.
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DR EMBL; GG705057; EEY90590.1; -; Genomic_DNA.
DR RefSeq; WP_004279435.1; NZ_GG705057.1.
DR AlphaFoldDB; D0SUN5; -.
DR GeneID; 69582756; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_0_0_6; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000018425; Unassembled WGS sequence.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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 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; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU361138};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361138};
KW Transferase {ECO:0000256|RuleBase:RU361138, ECO:0000313|EMBL:EEY90590.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU361138}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 118..155
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 404 AA; 43474 MW; F0C10519E774F85A CRC64;
MATEIKAPVF PESVADGTIA TWHKQPGEAV SRDEVICDIE TDKVVLEVVA PADGTLASII
KGEGDTVLSA EVIAQFEEGA VSGATQTQAV QSEEKVEQAA AQTEAGNAPI VERQQVQDQA
PAVRKALTES GVAAADVAGT GRGGRITKED VANHQAKPAA PAAQPLSVAV GERIEKRVPM
TRLRKRVAER LLAATQETAM LTTFNEVNMK PIMEMRAQYK DAFEKRHGAR LGFMSFFVKA
ATEALKRYPA VNASIDGDDI VYHGYYDIGV AVSSERGLVV PVLRDTDRMN YAEVENGIRA
YAGKARDGKL GIEDMTGGTF TITNGGTFGS LLSTPILNTP QTAILGMHKI QERPMAVNGQ
VEILPMMYLA LSYDHRLIDG KEAVGFLVTI KELLEEPARL ILDL
//