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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
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 (purA)
  2. Adenylosuccinate lyase (purB)
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. Phosphoribosylaminoimidazole-succinocarboxamide synthase (purC)
  2. Adenylosuccinate lyase (purB)
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

BioCyciMBUR259564:GHBZ-1181-MONOMER.
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
Name:purBImported
Ordered Locus Names:Mbur_1160Imported
OrganismiMethanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)Imported
Taxonomic identifieri259564 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides
Proteomesi
  • UP000001979 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi259564.Mbur_1160.

Structurei

3D structure databases

ProteinModelPortaliQ12WU3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini359 – 43981ADSL_CInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG01747. Archaea.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiAMILEHE.

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.

Q12WU3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIHPIEYRY GTDEMKYVWS EANRLEKLLK TEAALSNAEA KIGMVPAEAA
60 70 80 90 100
AEIEKSIAHV KIERVAEIED EIHHDMMAIV IAISEQCTDD AAKWVHFGAT
110 120 130 140 150
SNDILDTATA LQMMDAVAIL EEKTRTLLDV LLTKAEEHKN TVCAGRTHGQ
160 170 180 190 200
IGVPTTYGLR FAIWASEVAR HLERLAQLTP RLLVGQMTGA VGTQAAFGKD
210 220 230 240 250
GIEIQAHAME YLGLGSVDVS NQIIQRDRHA EFVMWMANTV TTLDKIAVEI
260 270 280 290 300
RTLQRSEIAE VEESFRKNQV GSSTMPHKRN PIKSEQISGL ARIVRSMVEP
310 320 330 340 350
ELLNNTLWDE RDLTNSSCER IVFPESCVLT DHLLKLAIGV IENLRFYPEN
360 370 380 390 400
IRKNLDLLRG LNMGEAIMID LAKRGVGRQE AHEIVRSSAM EAHESGKHLK
410 420 430 440
DVLLSRPDVT KYLNESEIND LLDPDMYIGT AVAQVENVVA KLRAQL
Length:446
Mass (Da):49,776
Last modified:August 22, 2006 - v1
Checksum:iFF7437B1374BDA22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000300 Genomic DNA. Translation: ABE52083.1.
RefSeqiWP_011499230.1. NC_007955.1.

Genome annotation databases

EnsemblBacteriaiABE52083; ABE52083; Mbur_1160.
GeneIDi3998446.
KEGGimbu:Mbur_1160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000300 Genomic DNA. Translation: ABE52083.1.
RefSeqiWP_011499230.1. NC_007955.1.

3D structure databases

ProteinModelPortaliQ12WU3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi259564.Mbur_1160.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE52083; ABE52083; Mbur_1160.
GeneIDi3998446.
KEGGimbu:Mbur_1160.

Phylogenomic databases

eggNOGiarCOG01747. Archaea.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiAMILEHE.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciMBUR259564:GHBZ-1181-MONOMER.

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...

Entry informationi

Entry nameiQ12WU3_METBU
AccessioniPrimary (citable) accession number: Q12WU3
Entry historyi
Integrated into UniProtKB/TrEMBL: August 22, 2006
Last sequence update: August 22, 2006
Last modified: September 7, 2016
This is version 63 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.