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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Acaryochloris marina (strain MBIC 11017)
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

BioCyciAMAR329726:GCZJ-5151-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:AM1_5164Imported
OrganismiAcaryochloris marina (strain MBIC 11017)Imported
Taxonomic identifieri329726 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesAcaryochloris
Proteomesi
  • UP000000268 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi329726.AM1_5164.

Structurei

3D structure databases

ProteinModelPortaliB0C8H1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini349 – 43082ADSL_CInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
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.

B0C8H1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIERYTLPKM GDLWTDENKF RTWLQVEIAV CEAQAELGKI PADALATIKA
60 70 80 90 100
KANFDVKRIL EIEAEVKHDV IAFLTNVNEY VGEAGRYIHL GMTSSDVLDT
110 120 130 140 150
AIALQMVASL DILLPQLENL IQAIRYQAQQ HRQTVMVGRS HGIHAEPITL
160 170 180 190 200
GFKLAGWLAE MMRHRDRLIA AQKEVAVGQI SGAVGTYANI DPQIECLTCQ
210 220 230 240 250
KLGLQPEAAS TQVISRDRHA YYLNALALVA ASIERFAVEI RNLQRTDVLE
260 270 280 290 300
VEEFFSKGQK GSSAMPHKRN PIRSERLTGL ARVVRGYAMT GLENVALWHE
310 320 330 340 350
RDISHSSAER VIVPDAAILT HFMLVEITDL VKHLQVYPEN MKRNMNLYGG
360 370 380 390 400
VIFSQSVLLA LVDKGMVRED AYAIVQTHAH QAWNKEGGNF KAALSQDPQV
410 420 430
QKLLSAEELD HCFDPSRHLQ NLDQVYQRLD I
Length:431
Mass (Da):48,392
Last modified:February 26, 2008 - v1
Checksum:i87A6BC8532D8E7A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000828 Genomic DNA. Translation: ABW30126.1.
RefSeqiWP_012165388.1. NC_009925.1.

Genome annotation databases

EnsemblBacteriaiABW30126; ABW30126; AM1_5164.
KEGGiamr:AM1_5164.
PATRICi20624358. VBIAcaMar40141_4792.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000828 Genomic DNA. Translation: ABW30126.1.
RefSeqiWP_012165388.1. NC_009925.1.

3D structure databases

ProteinModelPortaliB0C8H1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi329726.AM1_5164.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABW30126; ABW30126; AM1_5164.
KEGGiamr:AM1_5164.
PATRICi20624358. VBIAcaMar40141_4792.

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
KOiK01756.
OMAiVQENAMK.
OrthoDBiEOG686NDB.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciAMAR329726:GCZJ-5151-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MBIC 11017Imported.

Entry informationi

Entry nameiB0C8H1_ACAM1
AccessioniPrimary (citable) accession number: B0C8H1
Entry historyi
Integrated into UniProtKB/TrEMBL: February 26, 2008
Last sequence update: February 26, 2008
Last modified: July 6, 2016
This is version 56 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.