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P20707

- ODO1_AZOVI

UniProt

P20707 - ODO1_AZOVI

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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

sucA

Organism
Azotobacter vinelandii
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).

Catalytic activityi

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

Cofactori

Thiamine pyrophosphate.

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

SABIO-RKP20707.

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:sucA
Synonyms:odhA
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9439432-oxoglutarate dehydrogenase E1 componentPRO_0000162186Add
BLAST

Proteomic databases

PRIDEiP20707.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP20707.
SMRiP20707. Positions 90-943.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR011603. 2oxoglutarate_DH_E1.
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.

P20707-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQDSVMQRMW NSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFEKLPA
60 70 80 90 100
EAGTSTDVPH APVRDQFVLL AKNQRRAQPV ATSSVSTEHE KKQVEVLRLI
110 120 130 140 150
QAYRTRGHQA SQLDPLGLWQ RTAPSDLSIT HYGLTNADLD TPFRTGELYI
160 170 180 190 200
GKEEATLREI LQALQETYCR TIGAEFTHIV DSEQRNWFAQ RLESVRGRPV
210 220 230 240 250
YSKEAKSHLL ERLSAAEGLE KYLGTKYPGT KRFGLEGGES LVPVVDEIIQ
260 270 280 290 300
RSGSYGTKEV VIGMAHRGRL NLLVNALGKN PRDLFDEFEG KHLVELGSGD
310 320 330 340 350
VKYHQGFSSN VMTSGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRVDA
360 370 380 390 400
TGEKVVPISI HGDSAFAGQG VVMETFQMSQ IRGYKTGGTI HIVVNNQVGF
410 420 430 440 450
TTSNPVDTRS TEYCTDPAKM IQAPVLHVNG DDPEAVLFVT QLAVDYRMQF
460 470 480 490 500
KRDVVIDLVC YRRRGHNEAD EPSGTQPLMY QKIAKQPTTR ELYADALVKE
510 520 530 540 550
GSLSQEEVQA KVDEYRTALD NGQHVLKSLV KEPNTELFVD WTPYLGHAWT
560 570 580 590 600
ARHDTSFELK TLQELNAKLL QIPEGFVVQR QVAKILEDRG RMGVGAMPIN
610 620 630 640 650
WGCAETLAYA TLLKEGHPVR ITGQDVGRGT FSHRHAALHN QKDASRYIPL
660 670 680 690 700
QNLYEGQPKF ELYDSFLSEE AVLAFEYGYA TTTPNALVIW EASSGDFANG
710 720 730 740 750
AQVVIDQFIS SGETKWGALC GLTMLLPHGY EGQGPEHSSA RLERYLQLCA
760 770 780 790 800
EQNIQVCVPT TPAQVYHMLR RQVIRPLRKP LVALTPKSLL RHKSAISTLE
810 820 830 840 850
DLALGSFHPV LPEVDSLDPK KVERLVLCSG KVYYDLLDKR HAEGREDIAI
860 870 880 890 900
VRIEQLYPFP EEELAEVMAP YTNLKHVVWC QEEPMNQGAW YCSQHHMRRV
910 920 930 940
ASAHKKELFL QYAGREASAA PACGYASMHA EQQEKLLQDA FTV
Length:943
Mass (Da):105,688
Last modified:February 1, 1991 - v1
Checksum:iD3F35356D454E2A1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52433 Genomic DNA. Translation: CAA36680.1.
X52432 Genomic DNA. Translation: CAA36677.1.
PIRiS07776.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52433 Genomic DNA. Translation: CAA36680.1 .
X52432 Genomic DNA. Translation: CAA36677.1 .
PIRi S07776.

3D structure databases

ProteinModelPortali P20707.
SMRi P20707. Positions 90-943.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P20707.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P20707.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
InterProi IPR011603. 2oxoglutarate_DH_E1.
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. "The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component."
    Schulze E., Westphal A.H., Hanemaaijer R., de Kok A.
    Eur. J. Biochem. 187:229-234(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component."
    Westphal A.H., de Kok A.
    Eur. J. Biochem. 187:235-239(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 909-943.

Entry informationi

Entry nameiODO1_AZOVI
AccessioniPrimary (citable) accession number: P20707
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 1, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3