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Protein
Submitted name:

2,5-dioxovalerate dehydrogenase (Alpha-ketoglutaric semialdehyde dehydrogenase)

Gene

BATR1942_19880

Organism
Bacillus atrophaeus (strain 1942)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein inferred from homologyi

Functioni

GO - Molecular functioni

  1. oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Enzyme and pathway databases

BioCyciBATR720555:GHTA-4019-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
2,5-dioxovalerate dehydrogenase (Alpha-ketoglutaric semialdehyde dehydrogenase)Imported
Gene namesi
Ordered Locus Names:BATR1942_19880Imported
OrganismiBacillus atrophaeus (strain 1942)Imported
Taxonomic identifieri720555 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000006867 Componenti: Chromosome

Structurei

3D structure databases

ProteinModelPortaliE3DTN2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000271511.
KOiK00128.
OMAiHLYQIAS.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E3DTN2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVMTEKNTY LNYINGAWVK SHSGDMVKVE NPADIHDLVG YVQNSTAEDV
60 70 80 90 100
DRAVAAANEA KAAWRKLSGA ERGQYLYKTA DIMEQRLDEI AACATREMGK
110 120 130 140 150
TLPEAKGETA RGIAILRYYA GEGMRKTGDV IPSTDKDALM FTTRVPLGVV
160 170 180 190 200
GVISPWNFPV AIPIWKMAPA LVYGNTVVIK PATETAITCA KIIACFEEAG
210 220 230 240 250
LPAGVINLVT GPGSVVGQGL AEHNGVNGIT FTGSNQVGKI IGQAALERGA
260 270 280 290 300
KYQLEMGGKN PIIVTNEADL DAAAEAAITG AFRSTGQKCT ATSRVIVQSK
310 320 330 340 350
VYDRFKEKLI QRTKDITIGN SLKEDVWMGP IASKNQLDHC LSYIEKGIQE
360 370 380 390 400
GASLLIGGEK LEAGDYQNGY YVQPAIFDNV TSDMTIAQEE IFGPVIALLK
410 420 430 440 450
VGTMEEALDI ANDVKFGLSA SLFTQNIGHM LSFIDDIEAG LVRVNAESAG
460 470 480
VELQAPFGGL KQSSSHSREQ GEAAKDFFTA IKTVFIKQ
Length:488
Mass (Da):52,369
Last modified:January 11, 2011 - v1
Checksum:iA29E0E634136450B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002207 Genomic DNA. Translation: ADP34891.1.
RefSeqiYP_003975822.1. NC_014639.1.

Genome annotation databases

EnsemblBacteriaiADP34891; ADP34891; BATR1942_19880.
KEGGibae:BATR1942_19880.
PATRICi42575005. VBIBacAtr152324_4072.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002207 Genomic DNA. Translation: ADP34891.1.
RefSeqiYP_003975822.1. NC_014639.1.

3D structure databases

ProteinModelPortaliE3DTN2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADP34891; ADP34891; BATR1942_19880.
KEGGibae:BATR1942_19880.
PATRICi42575005. VBIBacAtr152324_4072.

Phylogenomic databases

HOGENOMiHOG000271511.
KOiK00128.
OMAiHLYQIAS.

Enzyme and pathway databases

BioCyciBATR720555:GHTA-4019-MONOMER.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genomic signatures of strain selection and enhancement in Bacillus atrophaeus subsp. Globigii, a historical biowarfare simulant."
    Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D., Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.
    , Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S., Rosenzweig C.N., Skowronski E.
    Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1942Imported.

Entry informationi

Entry nameiE3DTN2_BACA1
AccessioniPrimary (citable) accession number: E3DTN2
Entry historyi
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: April 1, 2015
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.