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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Coxiella burnetii (strain Dugway 5J108-111)
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

BioCyciCBUR434922:GJTP-948-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:CBUD_0889Imported
OrganismiCoxiella burnetii (strain Dugway 5J108-111)Imported
Taxonomic identifieri434922 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
Proteomesi
  • UP000008555 Componenti: Chromosome

Structurei

3D structure databases

ProteinModelPortaliA9KFH8.
SMRiA9KFH8. Positions 3-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 312299Lyase_1InterPro annotationAdd
BLAST
Domaini331 – 445115ASL_CInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000252916.
KOiK01756.
OMAiTFGKEMA.
OrthoDBiEOG686NDB.

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.

A9KFH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSPLTALS PLDGRYQNKV EALRPILSEY GLIRYRVIVE IKWLLFLSQE
60 70 80 90 100
KTLTEIPSLN DSDIKKLEEI IDHFDLQAAE AVKTIEATTN HDVKAVEYYL
110 120 130 140 150
QRQLEKEKNL APLIGFIHFG CTSEDINNLS YSLMINEARE IALIPIIKNI
160 170 180 190 200
GMRFQTLAEK YAELPLLSRT HGQPATPTTL GKELANIVAR IHAQYHSLAH
210 220 230 240 250
LKLLGKMNGA VGNFNAHQAA YPTFDWPTFS KRFIQSLGLE ANEYTTQIEP
260 270 280 290 300
HDRLSEFLQS LVRLNTILID CCRDIWSYIS LGYFFQKSKK NEVGSSTMPH
310 320 330 340 350
KVNPIDFENA EGNLGLANAL ANHLINKLPI SRWQRDLTDS TVMRNLGCIF
360 370 380 390 400
GYALIAYESL LKGLDKISAN EQRIREDLEA HSEVLAEALQ TVMRRYGVPR
410 420 430 440 450
AYEQLKELTR DKTIDKNRLT KFIEQLSLPT EAKNHLKSLT PSNYTGFAAE
460
LAKKISTFKW D
Length:461
Mass (Da):52,479
Last modified:February 5, 2008 - v1
Checksum:i5BE3F21D309ACCE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000733 Genomic DNA. Translation: ABS77912.1.
RefSeqiWP_005768896.1. NC_009727.1.

Genome annotation databases

EnsemblBacteriaiABS77912; ABS77912; CBUD_0889.
KEGGicbd:CBUD_0889.
PATRICi17921620. VBICoxBur32972_0916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000733 Genomic DNA. Translation: ABS77912.1.
RefSeqiWP_005768896.1. NC_009727.1.

3D structure databases

ProteinModelPortaliA9KFH8.
SMRiA9KFH8. Positions 3-456.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS77912; ABS77912; CBUD_0889.
KEGGicbd:CBUD_0889.
PATRICi17921620. VBICoxBur32972_0916.

Phylogenomic databases

HOGENOMiHOG000252916.
KOiK01756.
OMAiTFGKEMA.
OrthoDBiEOG686NDB.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciCBUR434922:GJTP-948-MONOMER.

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...

Publicationsi

  1. "Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
    Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J.III., Porcella S.F., Samuel J.E., Heinzen R.A.
    Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Dugway 5J108-111Imported.

Entry informationi

Entry nameiA9KFH8_COXBN
AccessioniPrimary (citable) accession number: A9KFH8
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: July 6, 2016
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete 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.