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Protein

Adenylosuccinate lyase

Gene

Tb09.160.5560

Organism
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei185 – 1851AMPCombined sources
Binding sitei262 – 2621AMPCombined sources
Metal bindingi285 – 2851MagnesiumCombined sources
Metal bindingi289 – 2891MagnesiumCombined sources
Binding sitei324 – 3241AMPCombined sources
Metal bindingi346 – 3461Magnesium; via carbonyl oxygenCombined sources
Metal bindingi348 – 3481Magnesium; via carbonyl oxygenCombined sources
Binding sitei350 – 3501AMPCombined sources
Binding sitei355 – 3551AMPCombined sources
Binding sitei359 – 3591AMPCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 302AMPCombined sources
Nucleotide bindingi106 – 1083AMPCombined sources

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. metal ion binding Source: UniProtKB-KW
  3. N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Source: UniProtKB-EC
  4. nucleotide binding Source: UniProtKB-KW

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

LyaseUniRule annotationImported

Keywords - Biological processi

Purine biosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumCombined sources, Metal-bindingCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyaseUniRule annotation (EC:4.3.2.2UniRule annotation)
Short name:
ASLUniRule annotation
Alternative name(s):
AdenylosuccinaseUniRule annotation
Gene namesi
ORF Names:Tb09.160.5560Imported
OrganismiTrypanosoma brucei brucei (strain 927/4 GUTat10.1)Imported
Taxonomic identifieri185431 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma
ProteomesiUP000008524: Chromosome 9

Interactioni

Protein-protein interaction databases

STRINGi5691.Tb09.160.5560.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EFCX-ray2.00A/B1-471[»]
ProteinModelPortaliQ38EJ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0015.
HOGENOMiHOG000252916.
InParanoidiQ38EJ2.
KOiK01756.
OMAiITPFTYV.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
IPR013539. PurB_C.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF08328. ASL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q38EJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKGSPSDLN GVDYSVDNPL FALSPLDGRY KRQTKALRAF FSEYGFFRYR
60 70 80 90 100
VLVEVEYFTA LCKDVPTIVP LRSVTDEQLQ KLRKITLDCF SVSSAEEIKR
110 120 130 140 150
LERVTNHDIK AVEYFIKERM DTCGLSHVTE FVHFGLTSQD INNTAIPMMI
160 170 180 190 200
RDAIVTLYLP ALDGIIGSLT SKLVDWDVPM LARTHGQPAS PTNLAKEFVV
210 220 230 240 250
WIERLREQRR QLCEVPTTGK FGGATGNFNA HLVAYPSVNW RAFADMFLAK
260 270 280 290 300
YLGLKRQQAT TQIENYDHLA ALCDACARLH VILIDMCRDV WQYISMGFFK
310 320 330 340 350
QKVKEGEVGS STMPHKVNPI DFENAEGNLA LSNALLNFFA SKLPISRLQR
360 370 380 390 400
DLTDSTVLRN LGVPIGHACV AFASISQGLE KLMISRETIS RELSSNWAVV
410 420 430 440 450
AEGIQTVLRR ECYPKPYETL KKLTQGNTDV TEEQVRNFIN GLTDISDDVR
460 470
AELLAITPFT YVGYVPRFSA K
Length:471
Mass (Da):53,120
Last modified:November 22, 2005 - v1
Checksum:iB3B15E435CF9DE3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000207 Genomic DNA. Translation: EAN76778.1.
RefSeqiXP_827108.1. XM_822015.1.

Genome annotation databases

GeneIDi3660448.
KEGGitbr:Tb09.160.5560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000207 Genomic DNA. Translation: EAN76778.1.
RefSeqiXP_827108.1. XM_822015.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EFCX-ray2.00A/B1-471[»]
ProteinModelPortaliQ38EJ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5691.Tb09.160.5560.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3660448.
KEGGitbr:Tb09.160.5560.

Phylogenomic databases

eggNOGiCOG0015.
HOGENOMiHOG000252916.
InParanoidiQ38EJ2.
KOiK01756.
OMAiITPFTYV.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
IPR013539. PurB_C.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF08328. ASL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of the African trypanosome Trypanosoma brucei."
    Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H., Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U., Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B., Alsmark U.C.M.
    , Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F., Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C., Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A., Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D., Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D., Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S., Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S., Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G., Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A., Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M., Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S., Walker D., Wanless D., Wang S., White B., White O., Whitehead S., Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E., Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E., Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.
    Science 309:416-422(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 927/4 GUTat10.1Imported.
  2. "Crystal Structure of Adenylosuccinate Lyase from Trypanosoma Brucei, Tb427tmp.160.5560."
    Wernimont A.K., Loppnau P., Osman K.T., Arrowsmith C.H., Edwards A.M., Bountra C., Robinson D.A., Wyatt P.G., Gilbert I.H., Hui R., Lin Y.H.
    Submitted (MAR-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH AMP AND MAGNESIUM.

Entry informationi

Entry nameiQ38EJ2_TRYB2
AccessioniPrimary (citable) accession number: Q38EJ2
Entry historyi
Integrated into UniProtKB/TrEMBL: November 22, 2005
Last sequence update: November 22, 2005
Last modified: March 4, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference 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.