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Database: UniProt
Entry: A0A149W0G2_9PROT
LinkDB: A0A149W0G2_9PROT
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ID   A0A149W0G2_9PROT        Unreviewed;       388 AA.
AC   A0A149W0G2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   31-JUL-2019, entry version 16.
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   Name=sucB {ECO:0000313|EMBL:KXW58962.1};
GN   ORFNames=FEMY_04840 {ECO:0000313|EMBL:KXW58962.1};
OS   Ferrovum sp. Z-31.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Ferrovales; Ferrovaceae;
OC   Ferrovum.
OX   NCBI_TaxID=1789004 {ECO:0000313|EMBL:KXW58962.1, ECO:0000313|Proteomes:UP000075653};
RN   [1] {ECO:0000313|EMBL:KXW58962.1, ECO:0000313|Proteomes:UP000075653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z-31 {ECO:0000313|EMBL:KXW58962.1,
RC   ECO:0000313|Proteomes:UP000075653};
RA   Poehlein A., Ullrich S.R., Schloemann M., Muehling M., Daniel R.;
RT   "Genome sequence of the acidophilic iron oxidising Ferrovum strain Z-
RT   31.";
RL   Submitted (JAN-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   -!- 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:KXW58962.1}.
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DR   EMBL; LRRD01000007; KXW58962.1; -; Genomic_DNA.
DR   RefSeq; WP_062187491.1; NZ_LRRD01000007.1.
DR   EnsemblBacteria; KXW58962; KXW58962; FEMY_04840.
DR   PATRIC; fig|1789004.3.peg.483; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000075653; 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   ECO:0000313|EMBL:KXW58962.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000075653};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075653};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:KXW58962.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN       98    135       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION      110    164       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    140    155       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   388 AA;  41997 MW;  35500CD42E436BFE CRC64;
     MSLEIKVPPL AESITEATVL AWHVVEGAPV QRDQKLVDIE TDKVVLEVPA PRAGVLQRIL
     KGVGNKVQSH EVLALMEEGQ DSSTVPLPAA TVPEAPVLVM PAASKILREQ GREPSVKGGS
     GRGGRILKED VIQDPTSGQV EPAGVETSSS LLPGAPRQER RTPLSALRRR VAERLMASQS
     GTATLTTFNE VDMSAVLALR QRYKDSFEKK HGIRLGLMSF FVKAVVSALQ RYPVLNARIE
     GTDWVTPEFI DIGVAIGSKR GLLVPILRDA QRLSMADIER QIADFSQRAD AGHITLAELS
     GGTFSITNGG VFGSMLSTPI LNPPQSAILG IHATRDRPMV VEGEIVIRPM NYLALSYDHR
     LIDGREAVLG LVAMKEGLED PARWLLDL
//
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