ODO2_BARQU
ID ODO2_BARQU Reviewed; 410 AA.
AC Q6FYD4; Q8GCX9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE EC=2.3.1.61 {ECO:0000250|UniProtKB:P0AFG6};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2;
DE Short=OGDC-E2;
DE AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
GN Name=sucB; OrderedLocusNames=BQ13410;
OS Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283165;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC VR-358 / Fuller / CIP 107027;
RX PubMed=12874367; DOI=10.1128/iai.71.8.4818-4822.2003;
RA Gilmore R.D. Jr., Carpio A.M., Kosoy M.Y., Gage K.L.;
RT "Molecular characterization of the sucB gene encoding the immunogenic
RT dihydrolipoamide succinyltransferase protein of Bartonella vinsonii subsp.
RT berkhoffii and Bartonella quintana.";
RL Infect. Immun. 71:4818-4822(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Toulouse;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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:0000250|UniProtKB:P0AFG6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581,
CC Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000250|UniProtKB:P0AFG6};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Note=Binds 1 lipoyl cofactor covalently.;
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 6/6.
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex
CC composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide
CC succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the
CC complex contains multiple copies of the three enzymatic components (E1,
CC E2 and E3). {ECO:0000250|UniProtKB:P0AFG6}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY160680; AAN78229.2; -; Genomic_DNA.
DR EMBL; BX897700; CAF26799.1; -; Genomic_DNA.
DR RefSeq; WP_011179953.1; NC_005955.1.
DR AlphaFoldDB; Q6FYD4; -.
DR SMR; Q6FYD4; -.
DR STRING; 283165.BQ13410; -.
DR PRIDE; Q6FYD4; -.
DR EnsemblBacteria; CAF26799; CAF26799; BQ13410.
DR KEGG; bqu:BQ13410; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_0_0_5; -.
DR OMA; MKVPSPG; -.
DR OrthoDB; 1626282at2; -.
DR BRENDA; 2.3.1.61; 7856.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000000597; Chromosome.
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: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 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 InterPro; IPR006255; SucB.
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 TIGRFAMs; TIGR01347; sucB; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipoyl; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..410
FT /note="Dihydrolipoyllysine-residue succinyltransferase
FT component of 2-oxoglutarate dehydrogenase complex"
FT /id="PRO_0000162257"
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 116..153
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 86..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 381
FT /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT ACT_SITE 385
FT /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT MOD_RES 43
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT CONFLICT 4
FT /note="G -> E (in Ref. 1; AAN78229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 43763 MW; 216936AE2432DC05 CRC64;
MTTGIRVPTL GESVTEATIG KWFKKLGEAV AVDEPLVELE TDKVTVEVPS PVMGKLTEII
AKEGDIVEVN AVLGFVESGA AGISQSFSPS ATSIPEAPSE LEQSPSSSAT PSGTMPPAPS
AAKLMAENNI AKSDISGSGK RGQILKEDVL GALAQGTKAS TSVATLTASS SSAAPIQEMR
EERVRMTKLR QTIARRLKDA QNTAAMLTTF NEVDMSAVMD LRKRYKDLFE KKHGVKLGFM
GFFTKAVCHA LKEFPTVNAE IDGTDIVYKN YVNAGIAVGT DKGLVVPVVR DADQMSLAEI
EKEISRLGRL ARDGKLAVSD MQGGTFTITN GGVYGSLMST PILNAPQSGI LGMHAIKERA
MVVGGQIIIC PMMYLALSYD HRIVDGQEAV TFLVRVKESL EDPERLVLDL
