adhE:Gene Product(s) - EcoliWiki
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adhE:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

AdhE

Synonyms

fused acetaldehyde-CoA dehydrogenase[1], iron-dependent alcohol dehydrogenase[1], pyruvate-formate lyase deactivase[1], B1241[2][1], AdhC[2][1], Ana[2][1], AdhE[2][1]

Product description

AdhE[2][3];

Component of ; ADHE-CPLX[2]

EC number (for enzymes)
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Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0003824

catalytic activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0511

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0004022

alcohol dehydrogenase activity

GO_REF:0000002
GO_REF:0000003

IEA: Inferred from Electronic Annotation

InterPro:IPR012079
EC:1.1.1.1

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0046872

metal ion binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001670

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005506

iron ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0408

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0006066

cellular alcohol metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012079

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0008152

metabolic process

GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001670
InterPro:IPR015590

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0008774

acetaldehyde dehydrogenase (acetylating) activity

GO_REF:0000002
GO_REF:0000003

IEA: Inferred from Electronic Annotation

InterPro:IPR012079
EC:1.2.1.10

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0015976

carbon utilization

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012079

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0016491

oxidoreductase activity

GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR001670
InterPro:IPR015590
SP_KW:KW-0560

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P0A7V0

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005624

membrane fraction

PMID:16858726[6]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc 12.5 [4]

complete

GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

required fields missing

GO:0006113

fermentation

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0004022

alcohol dehydrogenase activity

PMID:6998946[7]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0008774

acetaldehyde dehydrogenase (acetylating) activity

PMID:6998946[7]

IMP: Inferred from Mutant Phenotype

F

complete

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Interactions

Partner TypePartnerNotesReferences

Protein

Subunits of ADHE-CPLX

could be indirect


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Notes

Localization

CompartmentDescriptionEvidenceNotes
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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc

MAVTNVAELN ALVERVKKAQ REYASFTQEQ VDKIFRAAAL AAADARIPLA KMAVAESGMG
IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDDTFGTITI AEPIGIICGI VPTTNPTSTA
IFKSLISLKT RNAIIFSPHP RAKDATNKAA DIVLQAAIAA GAPKDLIGWI DQPSVELSNA
LMHHPDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASVLMSKTF
DNGVICASEQ SVVVVDSVYD AVRERFATHG GYLLQGKELK AVQDVILKNG ALNAAIVGQP
AYKIAELAGF SVPENTKILI GEVTVVDESE PFAHEKLSPT LAMYRAKDFE DAVEKAEKLV
AMGGIGHTSC LYTDQDNQPA RVSYFGQKMK TARILINTPA SQGGIGDLYN FKLAPSLTLG
CGSWGGNSIS ENVGPKHLIN KKTVAKRAEN MLWHKLPKSI YFRRGSLPIA LDEVITDGHK
RALIVTDRFL FNNGYADQIT SVLKAAGVET EVFFEVEADP TLSIVRKGAE LANSFKPDVI
IALGGGSPMD AAKIMWVMYE HPETHFEELA LRFMDIRKRI YKFPKMGVKA KMIAVTTTSG
TGSEVTPFAV VTDDATGQKY PLADYALTPD MAIVDANLVM DMPKSLCAFG GLDAVTHAME
AYVSVLASEF SDGQALQALK LLKEYLPASY HEGSKNPVAR ERVHSAATIA GIAFANAFLG
VCHSMAHKLG SQFHIPHGLA NALLICNVIR YNANDNPTKQ TAFSQYDRPQ ARRRYAEIAD
HLGLSAPGDR TAAKIEKLLA WLETLKAELG IPKSIREAGV QEADFLANVD KLSEDAFDDQ
CTGANPRYPL ISELKQILLD TYYGRDYVEG ETAAKKEAAP AKAEKKAKKS A
Mol. Wt

96.13 kDa (calc) [2]

pI

6.72[2]

Extinction coefficient

69220 - 70345 (calc based on 28 Y, 5 W, and 9 C residues)

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Domains/Motifs/Modification Sites

TypeResiduesDescriptionNotes
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Structure

Structures
  • Representative homolog:
    1O2D|A (Thermotoga maritima)
    41-242 of 891 residues (E-value: 1.3e-19) (Percent Identity: 31.34)
  • View all other structures.
Models

View models at:

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Notes

Gene Product Resources

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Resource typeSourceNotes/Reference
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Notes

Accessions in Other Databases

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DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:ADHE-MONOMER

UniProt (EcoliWiki Page)

UniProt:P0A9Q7

PFAM (EcoliWiki Page)

PFAM:PF00465

RefSeq (EcoliWiki Page)

RefSeq:NP_415757

ModBase (EcoliWiki Page)

ModBase:P0A9Q7


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Notes

Links

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NameURLComments
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References

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See Help:References for how to manage references in EcoliWiki.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  5. Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed EcoliWiki page
  6. Lasserre JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27: 3306-21 PubMed EcoliWiki page
  7. 7.0 7.1 Clark DP & Cronan JE Jr (1980) Acetaldehyde coenzyme A dehydrogenase of Escherichia coli. J Bacteriol 144: 179-84 PubMed EcoliWiki page


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