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Q72PJ7

- ODO1_LEPIC

UniProt

Q72PJ7 - ODO1_LEPIC

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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

sucA

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
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).UniRule annotation

Catalytic activityi

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

Cofactori

Thiamine pyrophosphate.UniRule 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

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciLINT267671:GHQI-2467-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase E1 componentUniRule annotation (EC:1.2.4.2UniRule annotation)
Alternative name(s):
Alpha-ketoglutarate dehydrogenaseUniRule annotation
Gene namesi
Name:sucAUniRule annotation
Synonyms:odhAUniRule annotation
Ordered Locus Names:LIC_12474
OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Taxonomic identifieri267671 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
ProteomesiUP000007037: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9209202-oxoglutarate dehydrogenase E1 componentPRO_0000162173Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi267671.LIC12474.

Structurei

3D structure databases

ProteinModelPortaliQ72PJ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

Phylogenomic databases

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.

Q72PJ7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIEKLMALY GENGALLEEL YNQYKLNPET LDKEWKSFFQ EVDTNGLANG
60 70 80 90 100
SGYTNGNGKS AVATSFTDAQ AASIREMGII NLLNAYRRQG HLAAKLDPLG
110 120 130 140 150
IQKPNRTFID SKLHNISPAD IDTVVDSETL GRVKLAEIVD LYEKVYCNTI
160 170 180 190 200
GAEHFYLVND EEREWLQKKM ESPEFLAPLP RGIKLRLFEK LFQADYFETF
210 220 230 240 250
LAKKYVGKKR FSLEGGESFI PLLDTIVEEA GYHQMDGLVI GMAHRGRLNV
260 270 280 290 300
LVNIIEKPAS LIFAEFEEKT DKDNLSYADV KYHLGYSNSR MTTSGKEVKL
310 320 330 340 350
SLAFNPSHLE CVDPVVTGSV RARQTLIGDK DRSKYMPILI HGDAAFAGQG
360 370 380 390 400
VVAETLNLMN LEGYTTGGTF HIVVNNQIGF TTLPDESRST LYATDLAKGF
410 420 430 440 450
QIPIIHVNGD DPEAVYRVVK LGMEYRQKFK KDFIIDLVCY RRLGHNETDE
460 470 480 490 500
PAFTQPKMYA IIKNHPPTVK LYEKRLVEEG DIPQEDIDFI KNGSMHGLED
510 520 530 540 550
SFQRAKEQDV KIRVDTMQGV WSKFSKDSLD SEPATKLLAE QMHGIVQALT
560 570 580 590 600
SVPQGFTPNS KLVKLLQSRK EMAEGKIPVD WGFAEALSFG SILESGFRIR
610 620 630 640 650
LSGQDSQRGT FSHRHAVLVD TNTNEKYIPL NHISSKQAKA EIINSSLSEF
660 670 680 690 700
SVLGFEYGYS LSDPNALVMW EAQFGDFANS AQVIFDQFIS SSEVKWQRLS
710 720 730 740 750
GLIMLLPHGY EGQGPEHSSA RLERFLQLCA LDNMQVCNLT TAAQYFHLLR
760 770 780 790 800
RQMLRNYRKP LVIVTPKSLL RFPASLSPVE DILQGAFREI LIDDSGSKPD
810 820 830 840 850
KIEKVVFSAG KVYYDLMKYK DENKIKNVAL VRVEQIYPFP AKEIQSSLKT
860 870 880 890 900
FKNAKQFVWC QEEPKNQGAW FFVRERIEEL LPGNARLVYA GRHESPSPAA
910 920
GHMKLHLQEQ DQLVLDAFQA
Length:920
Mass (Da):103,922
Last modified:July 5, 2004 - v1
Checksum:i8A4513F3F1B3DD0A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016823 Genomic DNA. Translation: AAS71039.1.
RefSeqiYP_002402.1. NC_005823.1.

Genome annotation databases

EnsemblBacteriaiAAS71039; AAS71039; LIC_12474.
GeneIDi2770761.
KEGGilic:LIC12474.
PATRICi22377606. VBILepInt6257_2961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016823 Genomic DNA. Translation: AAS71039.1 .
RefSeqi YP_002402.1. NC_005823.1.

3D structure databases

ProteinModelPortali Q72PJ7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 267671.LIC12474.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAS71039 ; AAS71039 ; LIC_12474 .
GeneIDi 2770761.
KEGGi lic:LIC12474.
PATRICi 22377606. VBILepInt6257_2961.

Phylogenomic databases

KOi K00164.
OMAi GHQNANL.
OrthoDBi EOG6V1M1F.

Enzyme and pathway databases

BioCyci LINT267671:GHQI-2467-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. "Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis."
    Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S.
    , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.
    J. Bacteriol. 186:2164-2172(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Fiocruz L1-130.

Entry informationi

Entry nameiODO1_LEPIC
AccessioniPrimary (citable) accession number: Q72PJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: July 5, 2004
Last modified: October 1, 2014
This is version 65 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