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A0LIL1

- KAD_SYNFM

UniProt

A0LIL1 - KAD_SYNFM

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Protein

Adenylate kinase

Gene

adk

Organism
Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.UniRule annotation

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311AMPUniRule annotation
Binding sitei36 – 361AMPUniRule annotation
Binding sitei92 – 921AMPUniRule annotation
Binding sitei127 – 1271ATPUniRule annotation
Metal bindingi130 – 1301Zinc; structuralUniRule annotation
Metal bindingi133 – 1331Zinc; structuralUniRule annotation
Metal bindingi150 – 1501Zinc; structuralUniRule annotation
Metal bindingi153 – 1531Zinc; structuralUniRule annotation
Binding sitei160 – 1601AMPUniRule annotation
Binding sitei171 – 1711AMPUniRule annotation
Binding sitei199 – 1991ATP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156ATPUniRule annotation
Nucleotide bindingi57 – 593AMPUniRule annotation
Nucleotide bindingi85 – 884AMPUniRule annotation

GO - Molecular functioni

  1. adenylate kinase activity Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-HAMAP
  3. nucleic acid binding Source: InterPro
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. AMP salvage Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciSFUM335543:GH6P-1607-MONOMER.
UniPathwayiUPA00588; UER00649.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinaseUniRule annotation (EC:2.7.4.3UniRule annotation)
Short name:
AKUniRule annotation
Alternative name(s):
ATP-AMP transphosphorylaseUniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
Gene namesi
Name:adkUniRule annotation
Ordered Locus Names:Sfum_1576
OrganismiSyntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
Taxonomic identifieri335543 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophobacteraceaeSyntrophobacter
ProteomesiUP000001784: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213Adenylate kinasePRO_1000021776Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi335543.Sfum_1576.

Structurei

3D structure databases

ProteinModelPortaliA0LIL1.
SMRiA0LIL1. Positions 1-212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 5930NMPbindUniRule annotationAdd
BLAST
Regioni126 – 16338LIDUniRule annotationAdd
BLAST

Domaini

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.UniRule annotation

Sequence similaritiesi

Belongs to the adenylate kinase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0563.
HOGENOMiHOG000238772.
KOiK00939.
OMAiLMKSCID.
OrthoDBiEOG679TH4.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
IPR001878. Znf_CCHC.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SMARTiSM00343. ZnF_C2HC. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0LIL1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIILLGPPG AGKGTQASRL IGKYAIPQIS TGDMLRAALK EGTPLGLEAK
60 70 80 90 100
KYMDQGALVP DSVVIGLVKE RIQKPDCSKG YMLDGFPRNV SQAEALDMML
110 120 130 140 150
GELKQRIDGV VCIEVPNKEL LGRLTGRRTC RSCGAGFHVM FDPPKTDGKC
160 170 180 190 200
DKCGGELYQR DDDNEATVSS RLKVYEDQTK PLIDYYEKQG KLRRIDGVGS
210
MDAIFGRITA ILG
Length:213
Mass (Da):23,226
Last modified:December 12, 2006 - v1
Checksum:i455B36B689579F3E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000478 Genomic DNA. Translation: ABK17263.1.
RefSeqiYP_845698.1. NC_008554.1.

Genome annotation databases

EnsemblBacteriaiABK17263; ABK17263; Sfum_1576.
GeneIDi4460146.
KEGGisfu:Sfum_1576.
PATRICi23848531. VBISynFum78438_1839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000478 Genomic DNA. Translation: ABK17263.1 .
RefSeqi YP_845698.1. NC_008554.1.

3D structure databases

ProteinModelPortali A0LIL1.
SMRi A0LIL1. Positions 1-212.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 335543.Sfum_1576.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK17263 ; ABK17263 ; Sfum_1576 .
GeneIDi 4460146.
KEGGi sfu:Sfum_1576.
PATRICi 23848531. VBISynFum78438_1839.

Phylogenomic databases

eggNOGi COG0563.
HOGENOMi HOG000238772.
KOi K00939.
OMAi LMKSCID.
OrthoDBi EOG679TH4.

Enzyme and pathway databases

UniPathwayi UPA00588 ; UER00649 .
BioCyci SFUM335543:GH6P-1607-MONOMER.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00235. Adenylate_kinase_Adk.
InterProi IPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
IPR001878. Znf_CCHC.
[Graphical view ]
PANTHERi PTHR23359. PTHR23359. 1 hit.
Pfami PF05191. ADK_lid. 1 hit.
[Graphical view ]
PRINTSi PR00094. ADENYLTKNASE.
SMARTi SM00343. ZnF_C2HC. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01351. adk. 1 hit.
PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 10017 / MPOB.

Entry informationi

Entry nameiKAD_SYNFM
AccessioniPrimary (citable) accession number: A0LIL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: October 29, 2014
This is version 58 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3