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Database: UniProt
Entry: A0A1H4B5M1_9BACT
LinkDB: A0A1H4B5M1_9BACT
Original site: A0A1H4B5M1_9BACT 
ID   A0A1H4B5M1_9BACT        Unreviewed;       509 AA.
AC   A0A1H4B5M1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 10.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|RuleBase:RU361138};
DE            EC=2.3.1.61 {ECO:0000256|RuleBase:RU361138};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|RuleBase:RU361138};
GN   ORFNames=SAMN05192529_11867 {ECO:0000313|EMBL:SEA43503.1};
OS   Arachidicoccus rhizosphaerae.
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Arachidicoccus.
OX   NCBI_TaxID=551991 {ECO:0000313|EMBL:SEA43503.1, ECO:0000313|Proteomes:UP000199041};
RN   [1] {ECO:0000313|EMBL:SEA43503.1, ECO:0000313|Proteomes:UP000199041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vu-144 {ECO:0000313|EMBL:SEA43503.1,
RC   ECO:0000313|Proteomes:UP000199041};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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).
CC       {ECO:0000256|RuleBase:RU361138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate
CC         dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-
CC         (S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate
CC         dehydrogenase complex component E2] + CoA; Xref=Rhea:RHEA:15213,
CC         Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120;
CC         EC=2.3.1.61; Evidence={ECO:0000256|RuleBase:RU361138};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via
CC       saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
CC       {ECO:0000256|RuleBase:RU361138}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361138}.
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DR   EMBL; FNQY01000018; SEA43503.1; -; Genomic_DNA.
DR   BioCyc; GCF_900107765:BLU80_RS14340-MONOMER; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000199041; 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   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; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   TIGRFAMs; TIGR01347; sucB; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199041};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199041};
KW   Transferase {ECO:0000256|RuleBase:RU361138};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        1     75       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      115    189       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      216    253       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       79    105       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1H4B5M1}.
SQ   SEQUENCE   509 AA;  54699 MW;  B8BCA3C3BB71AEC5 CRC64;
     MIDIKVPTVG ESISEVTLIK WVKKTGDYVN RDEVIAELES EKATFEVNAE QAGILQTVAE
     EEQTLQIGDV LAKIDETAAA PAPSTPASAS APAETPAAAP SAEPAATAEA VGKGVIDMTV
     PTIGESITEV TLVNYLKQDG DLVRRDEPIA ELESEKATFE LNAEESGKLS LVAKIDDVLQ
     IGDLVAKIDT DVAVPAATAA APKAQAPVTT IPNDLKASPV ASAIIADKHM DPSTIKATGH
     GGRIMKGDVL AALANPGKQT FAGQPLNSRN ERREKMSNLR KTISRRLVES KNTTAMLTTF
     NEVDMTRIME VRKQYKDKFK EQHGVGLGFM SFFSKACAIA LSEWPAVNAY IDGNELVYHD
     YADISIAVST PKGLTVPVMR NVESMSMADI EKTVVELATK ARNGKLGMEE LTGGTFTITN
     GGTFGSLLST PIINLPQSAI LGMHKIQERP MAIGGQVVIR PMMYVALSYD HRIIDGKESV
     SFLVRVKELL ENPELLLYSK DPVKALLEL
//
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