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A7X295

- ODO1_STAA1

UniProt

A7X295 - ODO1_STAA1

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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Staphylococcus aureus (strain Mu3 / ATCC 700698)
Status
Reviewed - Annotation score: 2 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).By similarity

Catalytic activityi

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

Cofactori

Thiamine pyrophosphate.By similarity

GO - Molecular functioni

  1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB-EC
  2. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
  2. tricarboxylic acid cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciSAUR418127:GJP9-1419-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.2)
Alternative name(s):
Alpha-ketoglutarate dehydrogenase
Gene namesi
Name:odhA
Ordered Locus Names:SAHV_1401
OrganismiStaphylococcus aureus (strain Mu3 / ATCC 700698)
Taxonomic identifieri418127 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000001130: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9329322-oxoglutarate dehydrogenase E1 componentPRO_0000313016Add
BLAST

Proteomic databases

PRIDEiA7X295.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi418127.SAHV_1401.

Structurei

3D structure databases

ProteinModelPortaliA7X295.
SMRiA7X295. Positions 71-929.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
KOiK00164.
OMAiGHQNANL.
OrthoDBiEOG6V1M1F.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
HAMAPiMF_01169. SucA_OdhA.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR023784. 2oxoglutarate_DH_E1_bac.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

Sequencei

Sequence statusi: Complete.

A7X295-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKND
60 70 80 90 100
DSIVPALKST SSQNSDGTIK RVMRLIDNIR QYGHLKADIY PVNPPKRKHV
110 120 130 140 150
PKLEIEDFDL DQQTLEGISA GIVSDHFADI YDNAYEAILR MEKRYKGPIA
160 170 180 190 200
FEYTHINNNT ERGWLKRRIE TPYKVTLNNN EKRALFKQLA YVEGFEKYLH
210 220 230 240 250
KNFVGAKRFS IEGVDALVPM LQRTITIAAK EGIKNIQIGM AHRGRLNVLT
260 270 280 290 300
HVLEKPYEMM ISEFMHTDPM KFLPEDGSLQ LTAGWTGDVK YHLGGIKTTD
310 320 330 340 350
SYGTMQRIAL ANNPSHLEIV APVVEGRTRA AQDDTQRAGA PTTDHHKAMP
360 370 380 390 400
IIIHGDAAYP GQGINFETMN LGNLKGYSTG GSLHIITNNR IGFTTEPIDA
410 420 430 440 450
RSTTYSTDVA KGYDVPIFHV NADDVEATIE AIDIAMEFRK EFHKDVVIDL
460 470 480 490 500
VGYRRFGHNE MDEPSITNPV PYQNIRKHDS VEYVFGKKLV NEGVISEDEM
510 520 530 540 550
HSFIEQVQKE LRQAHDKINK ADKMDNPDME KPAELALPLQ ADEQSFTFDH
560 570 580 590 600
LKEINDALLT YPDGFNILKK LNKVLEKRHE PFNKEDGLVD WAQAEQLAFA
610 620 630 640 650
TILQDGTPIR LTGQDSERGT FSHRHAVLHD EQTGETYTPL HHVPDQKATF
660 670 680 690 700
DIHNSPLSEA AVVGFEYGYN VENKKSFNIW EAQYGDFANM SQMIFDNFLF
710 720 730 740 750
SSRSKWGERS GLTLFLPHAY EGQGPEHSSA RLERFLQLAA ENNCTVVNLS
760 770 780 790 800
SSSNYFHLLR AQAASLDSEQ MRPLVVMSPK SLLRNKTVAK PIDEFTSGGF
810 820 830 840 850
EPILTESYQA DKVTKVILAT GKMFIDLKEA LAKNPDESVL LVAIERLYPF
860 870 880 890 900
PEEEIEALLA QLPNLEEVSW VQEEPKNQGA WLYVYPYVKV LVADKYDLSY
910 920 930
HGRIQRAAPA EGDGEIHKLV QNKIIENALK NN
Length:932
Mass (Da):105,357
Last modified:October 23, 2007 - v1
Checksum:iF671CE1A65ADAF6D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461T → I in CAD92197. 1 PublicationCurated
Sequence conflicti864 – 8641N → K in CAD92197. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ564530 Genomic DNA. Translation: CAD92197.1.
AP009324 Genomic DNA. Translation: BAF78284.1.
RefSeqiYP_001441991.1. NC_009782.1.

Genome annotation databases

EnsemblBacteriaiBAF78284; BAF78284; SAHV_1401.
GeneIDi5561127.
KEGGisaw:SAHV_1401.
PATRICi19557834. VBIStaAur127830_1434.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ564530 Genomic DNA. Translation: CAD92197.1 .
AP009324 Genomic DNA. Translation: BAF78284.1 .
RefSeqi YP_001441991.1. NC_009782.1.

3D structure databases

ProteinModelPortali A7X295.
SMRi A7X295. Positions 71-929.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 418127.SAHV_1401.

Proteomic databases

PRIDEi A7X295.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAF78284 ; BAF78284 ; SAHV_1401 .
GeneIDi 5561127.
KEGGi saw:SAHV_1401.
PATRICi 19557834. VBIStaAur127830_1434.

Phylogenomic databases

eggNOGi COG0567.
HOGENOMi HOG000259588.
KOi K00164.
OMAi GHQNANL.
OrthoDBi EOG6V1M1F.

Enzyme and pathway databases

BioCyci SAUR418127:GJP9-1419-MONOMER.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
HAMAPi MF_01169. SucA_OdhA.
InterProi IPR011603. 2oxoglutarate_DH_E1.
IPR023784. 2oxoglutarate_DH_E1_bac.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view ]
PANTHERi PTHR23152. PTHR23152. 1 hit.
Pfami PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic analysis of seventeen genes in Staphylococcus aureus with reduced susceptibility to vancomycin (VRSA) and hetero-VRSA (hVRSA)."
    Wootton M., Avison M.B., Bennett P.M., Howe R.A., MacGowan A.P., Walsh T.R.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Mutated response regulator graR is responsible for phenotypic conversion of Staphylococcus aureus from heterogeneous vancomycin-intermediate resistance to vancomycin-intermediate resistance."
    Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.
    Antimicrob. Agents Chemother. 52:45-53(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu3 / ATCC 700698.

Entry informationi

Entry nameiODO1_STAA1
AccessioniPrimary (citable) accession number: A7X295
Secondary accession number(s): Q7ASB7
, Q7WRM3, Q7WRN1, Q7WRX0, Q7WZ40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: October 1, 2014
This is version 48 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3