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Q4L6C3

- ODO2_STAHJ

UniProt

Q4L6C3 - ODO2_STAHJ

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Protein
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Gene
odhB, sucB, SH1493
Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Catalytic activityi

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei394 – 3941 By similarity
Active sitei398 – 3981 By similarity

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciSHAE279808:GJX7-1547-MONOMER.
UniPathwayiUPA00868; UER00840.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC:2.3.1.61)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name:
OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Gene namesi
Name:odhB
Synonyms:sucB
Ordered Locus Names:SH1493
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000543: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000288109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-lipoyllysine Reviewed prediction

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry By similarity.

Protein-protein interaction databases

STRINGi279808.SH1493.

Structurei

3D structure databases

ProteinModelPortaliQ4L6C3.
SMRiQ4L6C3. Positions 194-420.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7574Lipoyl-binding
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
KOiK00658.
OMAiQEDETVE.
OrthoDBiEOG610413.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4L6C3-1 [UniParc]FASTAAdd to Basket

« Hide

MPEVKVPELA ESITEGTIAE WLKNVGDSVE KGEAILELET DKVNVEVVSE    50
EEGVLQEQLA SEGDTVEVGQ VIATVGEGSG NASSSKEESS DQSQSANNDE 100
ATKELAQPTE SQSNNEETQS NPNNQRVNAT PSARRHAREN GVDLSTVSGK 150
GNDVVRKDDV ENSQKAAQSQ SSQETSKKEE PKKSSGAPNK PVIREKMSRR 200
KKTAAKKLLE VSNNTAMLTT FNEVDMTNVM ELRKRKKEQF IKDHDGTKLG 250
FMSFFTKAAV AALKKYPEVN AEIDGDDMIT KQYYDIGVAV STDDGLLVPF 300
VRDCDKKNFA ELERAIADLA VKARDKKLGL DDMVNGSFTI TNGGVFGSMM 350
STPIINGNQA AILGMHSIIT RPIAIDKDTI ENRPMMYIAL SYDHRIIDGK 400
EAVGFLKTIK ELIESPEDLL LES 423
Length:423
Mass (Da):46,249
Last modified:August 2, 2005 - v1
Checksum:iC1FD7CF93C4E1D88
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006716 Genomic DNA. Translation: BAE04802.1.
RefSeqiYP_253408.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE04802; BAE04802; SH1493.
GeneIDi3481999.
KEGGisha:SH1493.
PATRICi19619097. VBIStaHae67511_1472.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006716 Genomic DNA. Translation: BAE04802.1 .
RefSeqi YP_253408.1. NC_007168.1.

3D structure databases

ProteinModelPortali Q4L6C3.
SMRi Q4L6C3. Positions 194-420.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 279808.SH1493.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE04802 ; BAE04802 ; SH1493 .
GeneIDi 3481999.
KEGGi sha:SH1493.
PATRICi 19619097. VBIStaHae67511_1472.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281563.
KOi K00658.
OMAi QEDETVE.
OrthoDBi EOG610413.

Enzyme and pathway databases

UniPathwayi UPA00868 ; UER00840 .
BioCyci SHAE279808:GJX7-1547-MONOMER.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01347. sucB. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
    Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
    J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCSC1435.

Entry informationi

Entry nameiODO2_STAHJ
AccessioniPrimary (citable) accession number: Q4L6C3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: August 2, 2005
Last modified: May 14, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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