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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Bacillus anthracis
Status
Unreviewed-Annotation score: Annotation score: 2 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

Pathway: 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.

Pathway: 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

BioCyciANTHRA:PURB-MONOMER.
BANT260799:GJAJ-319-MONOMER.
BANT261594:GJ7F-328-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:GBAA_0290Imported
ORF Names:BF27_1666Imported
OrganismiBacillus anthracisImported
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000594 Componenti: Chromosome UP000031920 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi198094.BA_0290.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PFMX-ray2.00A/B1-435[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000033912.
KOiK01756.
OMAiPKNMLKN.
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.

Q81ZH6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISRYTRPEM GAIWTEENKF KAWLEVEILA CEAWAELGDI PKEDVKKIRE
60 70 80 90 100
HASFDIDRIY EIEKETRHDV VAFTRAVSET PALGEERKWV HYGLTSTDVV
110 120 130 140 150
DTALSYILKQ ANEIILKDLE NFVSILANKA KEHKYTIMMG RTHGVHAEPT
160 170 180 190 200
TFGLKLGLWY EEMKRNVERF KQAANTVRVG KLSGAVGTYA NIDPFVEKYV
210 220 230 240 250
CENLGLEAAP ISTQTLQRDR HAHYMSTLAL IATSIEKMAV EIRGLQKSET
260 270 280 290 300
REVEEAFAKG QKGSSAMPHK RNPIGSENMT GLARVIRGYM MTAYENVPLW
310 320 330 340 350
HERDISHSSA ERVILPDATI ALNYMLNRFG NIVKNLTVYP ENMKRNMTRT
360 370 380 390 400
YGLIYSQRVM LTLIDKGMVR EEAYDIVQPK AMEAWETQVQ FKELVEADER
410 420 430
ITSKLTQEEI NECFNYEHHM QHVDTIFERL GLNEA
Length:435
Mass (Da):49,988
Last modified:June 1, 2003 - v1
Checksum:i772B8EB811E0CB98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT29377.1.
CP009902 Genomic DNA. Translation: AJH88728.1.
RefSeqiNP_842840.1. NC_003997.3.
WP_000625683.1. NZ_KN050651.1.
YP_016902.1. NC_007530.2.
YP_026557.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP24326; AAP24326; BA_0290.
AAT29377; AAT29377; GBAA_0290.
AAT52608; AAT52608; BAS0277.
AIF54759; AIF54759; HYU01_01590.
AIK06400; AIK06400; DH23_0274.
AIK33986; AIK33986; DJ48_3917.
AIK51587; AIK51587; DJ45_5597.
AIK59043; AIK59043; DJ44_4150.
AJA84772; AJA84772; RT54_01645.
KFJ82778; KFJ82778; DJ42_4800.
KFL76796; KFL76796; DJ49_5204.
KFL79427; KFL79427; DJ43_4836.
KGZ45689; KGZ45689; OY21_21065.
KGZ54551; KGZ54551; OY22_04980.
KGZ57369; KGZ57369; NX97_02275.
KGZ65781; KGZ65781; OY24_20145.
KGZ72788; KGZ72788; OY25_00670.
KGZ73136; KGZ73136; OY23_03365.
KGZ85674; KGZ85674; OY26_06900.
KGZ86681; KGZ86681; OY28_08870.
KGZ88848; KGZ88848; OY27_03640.
KHA04016; KHA04016; OY30_03465.
KHA05720; KHA05720; OY29_02185.
KHA07838; KHA07838; OY32_02550.
KHA19244; KHA19244; OY36_18060.
KHA19457; KHA19457; OY34_01325.
KHA20381; KHA20381; OY35_02485.
KHA34277; KHA34277; OY38_08665.
KHA34288; KHA34288; OY37_01280.
KHA44001; KHA44001; OY39_02950.
KHA45131; KHA45131; OY40_04005.
KHG60469; KHG60469; OY33_01400.
KHG61833; KHG61833; OY31_00555.
KHG63209; KHG63209; OY20_06715.
GeneIDi1085703.
2850059.
KEGGiban:BA_0290.
bar:GBAA_0290.
bat:BAS0277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT29377.1.
CP009902 Genomic DNA. Translation: AJH88728.1.
RefSeqiNP_842840.1. NC_003997.3.
WP_000625683.1. NZ_KN050651.1.
YP_016902.1. NC_007530.2.
YP_026557.1. NC_005945.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PFMX-ray2.00A/B1-435[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_0290.

Protocols and materials databases

DNASUi1085703.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP24326; AAP24326; BA_0290.
AAT29377; AAT29377; GBAA_0290.
AAT52608; AAT52608; BAS0277.
AIF54759; AIF54759; HYU01_01590.
AIK06400; AIK06400; DH23_0274.
AIK33986; AIK33986; DJ48_3917.
AIK51587; AIK51587; DJ45_5597.
AIK59043; AIK59043; DJ44_4150.
AJA84772; AJA84772; RT54_01645.
KFJ82778; KFJ82778; DJ42_4800.
KFL76796; KFL76796; DJ49_5204.
KFL79427; KFL79427; DJ43_4836.
KGZ45689; KGZ45689; OY21_21065.
KGZ54551; KGZ54551; OY22_04980.
KGZ57369; KGZ57369; NX97_02275.
KGZ65781; KGZ65781; OY24_20145.
KGZ72788; KGZ72788; OY25_00670.
KGZ73136; KGZ73136; OY23_03365.
KGZ85674; KGZ85674; OY26_06900.
KGZ86681; KGZ86681; OY28_08870.
KGZ88848; KGZ88848; OY27_03640.
KHA04016; KHA04016; OY30_03465.
KHA05720; KHA05720; OY29_02185.
KHA07838; KHA07838; OY32_02550.
KHA19244; KHA19244; OY36_18060.
KHA19457; KHA19457; OY34_01325.
KHA20381; KHA20381; OY35_02485.
KHA34277; KHA34277; OY38_08665.
KHA34288; KHA34288; OY37_01280.
KHA44001; KHA44001; OY39_02950.
KHA45131; KHA45131; OY40_04005.
KHG60469; KHG60469; OY33_01400.
KHG61833; KHG61833; OY31_00555.
KHG63209; KHG63209; OY20_06715.
GeneIDi1085703.
2850059.
KEGGiban:BA_0290.
bar:GBAA_0290.
bat:BAS0277.

Phylogenomic databases

HOGENOMiHOG000033912.
KOiK01756.
OMAiPKNMLKN.
OrthoDBiEOG686NDB.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciANTHRA:PURB-MONOMER.
BANT260799:GJAJ-319-MONOMER.
BANT261594:GJ7F-328-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

« Hide 'large scale' publications
  1. "Crystal Structure of Adenylosuccinate Lyase (PurB) from Bacillus anthracis."
    Levdikov V.M., Blagova E.V., Wilkinson A.J., Wilson K.S.
    Submitted (APR-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestorImported and Ames AncestorImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 2002013094Imported.

Entry informationi

Entry nameiQ81ZH6_BACAN
AccessioniPrimary (citable) accession number: Q81ZH6
Secondary accession number(s): E9RC82
, E9RC83, Q6I4C3, Q6KY25
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 117 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.