Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B9EC10

- B9EC10_MACCJ

UniProt

B9EC10 - B9EC10_MACCJ

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Macrococcus caseolyticus (strain JCSC5402)
Status
Unreviewed - 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).UniRule annotationSAAS annotation

Catalytic activityi

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

Cofactori

Thiamine pyrophosphate.UniRule annotationSAAS annotation

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

OxidoreductaseUniRule annotationSAAS annotation

Keywords - Biological processi

GlycolysisUniRule annotationSAAS annotation

Keywords - Ligandi

Thiamine pyrophosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciMCAS458233:GI03-1075-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase E1 componentUniRule annotationSAAS annotation (EC:1.2.4.2UniRule annotationSAAS annotation)
Alternative name(s):
Alpha-ketoglutarate dehydrogenaseUniRule annotation
Gene namesi
Name:odhAUniRule annotation
Ordered Locus Names:MCCL_1064Imported
OrganismiMacrococcus caseolyticus (strain JCSC5402)Imported
Taxonomic identifieri458233 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesMacrococcus
ProteomesiUP000001383: Chromosome

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi458233.MCCL_1064.

Structurei

3D structure databases

ProteinModelPortaliB9EC10.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
KOiK00164.
OMAiQHAPNKE.
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.

B9EC10-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTKGKNLEEA PPRFGTNLGI LLEMFDQYQN DPSSVSDELQ ELFSNIQRGS
60 70 80 90 100
TGHSGMGSTD ADIVKRLMRL IDNIRQYGHL KADIYPLYKP KRDQHIKLSI
110 120 130 140 150
EDFGLSEEVL KQLPASLVSE HYGERLNNAF EAITEMQQTY QGPIAYEVSH
160 170 180 190 200
INNSEEREWL KTTIESKVKR DFSKEEKVEL LKSVARVEGF EKYIHKNFVG
210 220 230 240 250
AKRFSIEGVD ALVPMLENVI KFAGENNIQD IEIGMAHRGR LNVLTHILEK
260 270 280 290 300
PYEMMLSEFM HTDPMKFLPE DGSLVVKKGW TGDVKYHLGG IKTTTRFGKT
310 320 330 340 350
QTISLANNPS HLEIVAPVVL GKTRAVQEVT DGVNEPKQDF NKALAVLIHG
360 370 380 390 400
DAAFPGQGIN FESMNLSNLK GYSVGGSLHI ITNNRVGFTT ESYDSRSTTY
410 420 430 440 450
ATDVAKGYDL PIIHVNADDL EACIEAIEVA MAYRQKFNKD FVIDLVGYRR
460 470 480 490 500
YGHNEMDEPT VTNPMLYKEV KGHPSIEILY GKSLVEASVI TEDEMNAIFE
510 520 530 540 550
DVASRLRSAH DAIDKSSVNN DSEMKMPEAV EAGYEKIDTG VALEKLKQLN
560 570 580 590 600
DDMLSIPEQF SVFNKLQKIL ERRNDPFTKD GLVDWGHAEL LAYGTIIQDG
610 620 630 640 650
NPVRHTGQDA ERGTFAHRHA VLHDVKNGDK YIPLQHIEGA QSSFDIHNSP
660 670 680 690 700
LSEAAVVGFE YGYNLQNNKA LTVWEAQYGD FANMAQMIFD NFISSAEAKW
710 720 730 740 750
GEKSGLTLLL PHAYEGQGPE HSSARLERFL QLAAEHNWTV ANLSSTANYF
760 770 780 790 800
HLLRRQAQYL GTDRMRPLVI MSPKSLLRNS FVSDTIEKFT EGSFKAIISS
810 820 830 840 850
EYKKTKVKKL LIASGKVAVD LMTELTKNPN DEVHVIRLEQ IYPFPEQDIK
860 870 880 890 900
AIIDDLKGLT EIGFVQEEPK NQGSWHYIYP LLNNIKPAKV KLSYYGRPYR
910 920
AAPAEGDNEI HKIVQSKLIS EALNI
Length:925
Mass (Da):104,156
Last modified:March 24, 2009 - v1
Checksum:iCF4BA9E54754A667
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009484 Genomic DNA. Translation: BAH17771.1.
RefSeqiWP_012656969.1. NC_011999.1.
YP_002560467.1. NC_011999.1.

Genome annotation databases

EnsemblBacteriaiBAH17771; BAH17771; MCCL_1064.
GeneIDi7390741.
KEGGimcl:MCCL_1064.
PATRICi22424493. VBIMacCas48391_1189.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009484 Genomic DNA. Translation: BAH17771.1 .
RefSeqi WP_012656969.1. NC_011999.1.
YP_002560467.1. NC_011999.1.

3D structure databases

ProteinModelPortali B9EC10.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 458233.MCCL_1064.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAH17771 ; BAH17771 ; MCCL_1064 .
GeneIDi 7390741.
KEGGi mcl:MCCL_1064.
PATRICi 22424493. VBIMacCas48391_1189.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci MCAS458233:GI03-1075-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

  1. "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402, reflecting the ancestral genome of the human-pathogenic staphylococci."
    Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.
    J. Bacteriol. 191:1180-1190(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCSC5402Imported.

Entry informationi

Entry nameiB9EC10_MACCJ
AccessioniPrimary (citable) accession number: B9EC10
Entry historyi
Integrated into UniProtKB/TrEMBL: March 24, 2009
Last sequence update: March 24, 2009
Last modified: October 29, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3