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Database: UniProt
Entry: I4ZWX2_9GAMM
LinkDB: I4ZWX2_9GAMM
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ID   I4ZWX2_9GAMM            Unreviewed;       404 AA.
AC   I4ZWX2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   10-APR-2019, entry version 40.
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=HADU_00035 {ECO:0000313|EMBL:EIM40714.1};
OS   Acinetobacter sp. HA.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1173062 {ECO:0000313|EMBL:EIM40714.1, ECO:0000313|Proteomes:UP000018434};
RN   [1] {ECO:0000313|EMBL:EIM40714.1, ECO:0000313|Proteomes:UP000018434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HA {ECO:0000313|EMBL:EIM40714.1,
RC   ECO:0000313|Proteomes:UP000018434};
RX   PubMed=22933775; DOI=10.1128/JB.01194-12;
RA   Malhotra J., Dua A., Saxena A., Sangwan N., Mukherjee U., Pandey N.,
RA   Rajagopal R., Khurana P., Khurana J.P., Lal R.;
RT   "Genome Sequence of Acinetobacter sp. Strain HA, Isolated from the Gut
RT   of the Polyphagous Insect Pest Helicoverpa armigera.";
RL   J. Bacteriol. 194:5156-5156(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).
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   -!- 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
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EIM40714.1}.
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DR   EMBL; AJXD01000001; EIM40714.1; -; Genomic_DNA.
DR   RefSeq; WP_004810833.1; NZ_AJXD01000001.1.
DR   EnsemblBacteria; EIM40714; EIM40714; HADU_00035.
DR   GeneID; 34085639; -.
DR   PATRIC; fig|1173062.3.peg.7; -.
DR   BioCyc; ASP1173062:G10F2-1576-MONOMER; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000018434; 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; 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 {ECO:0000256|RuleBase:RU361138};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018434};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:EIM40714.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      118    155       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   404 AA;  43509 MW;  59F8FA0F11E89C27 CRC64;
     MATEIKAPVF PESVADGTIA TWHKQPGEAV SRDEVICDIE TDKVVLEVVA PADGTIASII
     KNEGDTVLSA EVIAQFEEGA VSGATQTQAV QSEEKVEQAA AQTEAGNSPI VERTQVADQA
     PAVRKALTES GIAASDVSGT GRGGRITKED VANHQAKPAA PAAAPLSVAV GERIEKRVPM
     TRLRKRVAER LLAATQETAM LTTFNEVNMK PIMEMRNQYK DAFEKRHGAR LGFMSFFVKA
     ATEALKRYPA VNASIDGDDI VYHGYYDIGV AVSSDRGLVV PVLRDTDRMN YAEVENGIRA
     YAGKAREGKL AIEDMTGGTF TITNGGTFGS LLSTPILNTP QTAILGMHKI QERPMAVNGQ
     VEILPMMYLA LSYDHRLIDG KEAVGFLVTI KELLEEPARL ILDL
//
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