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Protein

Adenylosuccinate lyase

Gene

LBRM_04_0500

Organism
Leishmania braziliensis
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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: AMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes AMP from IMP.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Adenylosuccinate synthetase (LbrM13_V2.0970)
  2. Adenylosuccinate lyase (LBRM_04_0500)
This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Adenylosuccinate lyase (LBRM_04_0500)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported

Keywords - Biological processi

Purine biosynthesisUniRule annotation

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:LBRM_04_0500Imported
OrganismiLeishmania braziliensisImported
Taxonomic identifieri5660 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmaniaLeishmania braziliensis species complex
Proteomesi
  • UP000007258 Componenti: Chromosome 4

Interactioni

Protein-protein interaction databases

STRINGi420245.XP_001561734.1.

Structurei

3D structure databases

ProteinModelPortaliA4H3W5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 339300Lyase_1InterPro annotationAdd
BLAST
Domaini358 – 474117ASL_CInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
InParanoidiA4H3W5.
KOiK01756.
OMAiTQVNPCD.

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.

A4H3W5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSSAQEAA ATATVTTTAH KVSAEISEDS PLFALSPLDG RYKHSTVPLR
60 70 80 90 100
AYFSEYALFK YRVQVEVLYF EALCKEVPTI TQLRGVTDAH LAQLRAATFE
110 120 130 140 150
NFTVDDATKI KDIEAVTKHD IKAVEYYLKD KMSACGLETE KEFIHFGLTS
160 170 180 190 200
QDINNTSIPM LLRDALHHHY IPALDQLIAL LKSKLPEWDV PMLARTHGQP
210 220 230 240 250
ASPTNLAKEF MVWIERLEEQ RAMLLSIPNT GKFGGATGNF NAHLCAYPGV
260 270 280 290 300
DWRNFGDLFL SKYLGLRRQR YTTQIEHYDN LAAICDACAR LHTILMDLAK
310 320 330 340 350
DVWQYISLGY FNQKVKAGEV GSSAMPHKVN PIDFENAEGN LGMSNAVLGF
360 370 380 390 400
LSAKLPISRL QRDLTDSTVL RNLGVPLSHA LIAFASLLRG VDKLLVNKPA
410 420 430 440 450
IAADLESNWA VVAEGIQTVL RREGYPKPYE ALKDLTRGNA QVTKETVRTF
460 470 480
IQQLEGITDE VRQELLAITP FTYVGYTRCL
Length:480
Mass (Da):53,584
Last modified:May 1, 2007 - v1
Checksum:iA8F1C77A8894CF1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR798978 Genomic DNA. Translation: CAM41527.1.
RefSeqiXP_001561734.1. XM_001561684.1.

Genome annotation databases

EnsemblProtistsiCAM41527; CAM41527; LBRM_04_0500.
GeneIDi5412684.
KEGGilbz:LBRM_04_0500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR798978 Genomic DNA. Translation: CAM41527.1.
RefSeqiXP_001561734.1. XM_001561684.1.

3D structure databases

ProteinModelPortaliA4H3W5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi420245.XP_001561734.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiCAM41527; CAM41527; LBRM_04_0500.
GeneIDi5412684.
KEGGilbz:LBRM_04_0500.

Phylogenomic databases

eggNOGiKOG2700. Eukaryota.
COG0015. LUCA.
InParanoidiA4H3W5.
KOiK01756.
OMAiTQVNPCD.

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...

Entry informationi

Entry nameiA4H3W5_LEIBR
AccessioniPrimary (citable) accession number: A4H3W5
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2007
Last sequence update: May 1, 2007
Last modified: September 7, 2016
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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 one 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.