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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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: AMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes AMP from IMP.
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.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Putative 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei145 – 1451Proton donor/acceptorBy similarity
Binding sitei219 – 2191SubstrateBy similarity
Active sitei269 – 2691Proton donor/acceptorBy similarity
Binding sitei308 – 3081SubstrateBy similarity
Binding sitei313 – 3131SubstrateBy similarity
Binding sitei317 – 3171SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-2289-MONOMER.
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:AF_2242
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Adenylosuccinate lyasePRO_0000137887Add
BLAST

Interactioni

Subunit structurei

Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site (By similarity).By similarity

Protein-protein interaction databases

STRINGi224325.AF2242.

Structurei

3D structure databases

ProteinModelPortaliO28041.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 102Substrate bindingBy similarity
Regioni73 – 753Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG01747. Archaea.
COG0015. LUCA.
KOiK01756.
OMAiVQENAMK.

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.

O28041-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVHPIDYRY GTPEMKRIWS EDSKIKRMVR VEMALLRALA KKGYLSEEEA
60 70 80 90 100
KEAKKKAYSV TPERVKEIEA EIKHDIMALV KAITEATGCR WVHFGATSND
110 120 130 140 150
IIDTATALQL RDSLKILEVK IKRLAKVLAD KALEYKDVVC LGRTHGQAAL
160 170 180 190 200
PTTYGFRFAL WAAEVARHYI RLQQMKDRLL VGQMSGAVGT QAAFGKDGFE
210 220 230 240 250
IEEEVMRLLN LKPALISSQI IPRDSYCEYL EFLANLAATL EKIALNFRLL
260 270 280 290 300
QRAEVGELME KFEAKQVGSS TMPHKRNPID CENVCGLARV VRGFVEPQHQ
310 320 330 340 350
SAILWEERDL TNSSAERITL VESTVLADHI LTKMIKVVSS VSLNLENIRR
360 370 380 390 400
NLEMQRGLNL SEAVMIEMTK RGVGRQEAHE ILRQAAMRAY ENNSSLLDEL
410 420 430 440
LKDERVMKYF KEDELREILK PENYLGTARE RVERVVRWVN EVLK
Length:444
Mass (Da):50,758
Last modified:January 1, 1998 - v1
Checksum:iA0F919725D4B813D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89013.1.
PIRiB69530.
RefSeqiWP_010879731.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB89013; AAB89013; AF_2242.
GeneIDi24796004.
KEGGiafu:AF_2242.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89013.1.
PIRiB69530.
RefSeqiWP_010879731.1. NC_000917.1.

3D structure databases

ProteinModelPortaliO28041.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF2242.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB89013; AAB89013; AF_2242.
GeneIDi24796004.
KEGGiafu:AF_2242.

Phylogenomic databases

eggNOGiarCOG01747. Archaea.
COG0015. LUCA.
KOiK01756.
OMAiVQENAMK.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciAFUL224325:GJBC-2289-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...

Publicationsi

  1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Entry informationi

Entry nameiPUR8_ARCFU
AccessioniPrimary (citable) accession number: O28041
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: November 11, 2015
This is version 112 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

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.