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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951SubstrateBy similarity
Active sitei141 – 1411Proton acceptor1 Publication
Active sitei141 – 1411Proton donor/acceptorBy similarity
Binding sitei212 – 2121SubstrateBy similarity
Active sitei262 – 2621Proton donor/acceptorBy similarity
Binding sitei301 – 3011SubstrateBy similarity
Binding sitei306 – 3061SubstrateBy similarity
Binding sitei310 – 3101SubstrateBy similarity

GO - Molecular functioni

  1. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Source: UniProtKB-EC
  2. N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Source: UniProtKB-EC

GO - Biological processi

  1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
  2. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BRENDAi4.3.2.2. 6331.
UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyase (EC:4.3.2.2)
Short name:
ASL
Alternative name(s):
Adenylosuccinase
Short name:
ASase
Gene namesi
Name:purB
Ordered Locus Names:TM_1095
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Adenylosuccinate lyasePRO_0000137886Add
BLAST

Interactioni

Subunit structurei

Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.1 Publication

Protein-protein interaction databases

STRINGi243274.TM1095.

Structurei

Secondary structure

1
431
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Helixi10 – 134Combined sources
Helixi16 – 3621Combined sources
Helixi44 – 518Combined sources
Helixi56 – 6611Combined sources
Helixi69 – 8113Combined sources
Helixi82 – 876Combined sources
Turni88 – 914Combined sources
Helixi94 – 13037Combined sources
Turni131 – 1333Combined sources
Beta strandi135 – 1406Combined sources
Beta strandi143 – 1497Combined sources
Helixi150 – 17425Combined sources
Beta strandi188 – 1903Combined sources
Helixi192 – 20110Combined sources
Beta strandi211 – 2133Combined sources
Helixi217 – 24327Combined sources
Turni246 – 2483Combined sources
Beta strandi250 – 2523Combined sources
Helixi272 – 28615Combined sources
Helixi288 – 2936Combined sources
Helixi304 – 33330Combined sources
Helixi338 – 3458Combined sources
Turni346 – 3505Combined sources
Helixi351 – 3533Combined sources
Helixi354 – 36310Combined sources
Helixi368 – 38316Combined sources
Beta strandi385 – 3873Combined sources
Helixi389 – 3946Combined sources
Helixi397 – 4004Combined sources
Helixi405 – 4106Combined sources
Helixi415 – 4184Combined sources
Helixi421 – 4266Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3CX-ray1.80A/B2-430[»]
1C3UX-ray2.30A/B1-431[»]
ProteinModelPortaliQ9X0I0.
SMRiQ9X0I0. Positions 2-430.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X0I0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 52Substrate bindingBy similarity
Regioni67 – 693Substrate bindingBy similarity
Regioni68 – 692Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0015.
InParanoidiQ9X0I0.
KOiK01756.
OMAiPKNMLKN.
OrthoDBiEOG686NDB.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9X0I0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVERYSLSPM KDLWTEEAKY RRWLEVELAV TRAYEELGMI PKGVTERIRN
60 70 80 90 100
NAKIDVELFK KIEEKTNHDV VAFVEGIGSM IGEDSRFFHY GLTSSDVLDT
110 120 130 140 150
ANSLALVEAG KILLESLKEF CDVLWEVANR YKHTPTIGRT HGVHAEPTSF
160 170 180 190 200
GLKVLGWYSE MKRNVQRLER AIEEVSYGKI SGAVGNYANV PPEVEEKALS
210 220 230 240 250
YLGLKPEPVS TQVVPRDRHA FYLSTLAIVA AGIERIAVEI RHLQRTEVLE
260 270 280 290 300
VEEPFRKGQR GSSAMPHKKN PITCERLTGL SRMMRAYVDP SLENIALWHE
310 320 330 340 350
RDISHSSVER YVFPDATQTL YYMIVTATNV VRNMKVNEER MKKNIDLTKG
360 370 380 390 400
LVFSQRVLLK LIEKGLTRKE AYDIVQRNAL KTWNSEKHFL EYLLEDEEVK
410 420 430
KLVTKEELEE LFDISYYLKH VDHIFERFEK E
Length:431
Mass (Da):49,873
Last modified:October 31, 1999 - v1
Checksum:iD3ACB25D87582869
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36171.1.
PIRiA72294.
RefSeqiNP_228901.1. NC_000853.1.
YP_007977450.1. NC_021214.1.
YP_008991807.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36171; AAD36171; TM_1095.
GeneIDi898670.
KEGGitma:TM1095.
tmi:THEMA_08870.
PATRICi23937125. VBITheMar51294_1111.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36171.1.
PIRiA72294.
RefSeqiNP_228901.1. NC_000853.1.
YP_007977450.1. NC_021214.1.
YP_008991807.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3CX-ray1.80A/B2-430[»]
1C3UX-ray2.30A/B1-431[»]
ProteinModelPortaliQ9X0I0.
SMRiQ9X0I0. Positions 2-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1095.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36171; AAD36171; TM_1095.
GeneIDi898670.
KEGGitma:TM1095.
tmi:THEMA_08870.
PATRICi23937125. VBITheMar51294_1111.

Phylogenomic databases

eggNOGiCOG0015.
InParanoidiQ9X0I0.
KOiK01756.
OMAiPKNMLKN.
OrthoDBiEOG686NDB.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BRENDAi4.3.2.2. 6331.

Miscellaneous databases

EvolutionaryTraceiQ9X0I0.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. "The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway."
    Toth E.A., Yeates T.O.
    Structure 8:163-174(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, ACTIVE SITE.

Entry informationi

Entry nameiPUR8_THEMA
AccessioniPrimary (citable) accession number: Q9X0I0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2000
Last sequence update: October 31, 1999
Last modified: March 31, 2015
This is version 119 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.