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Protein

Adenylosuccinate lyase

Gene

CKO_01840

Organism
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
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 (CKO_01840)
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 (CKO_01840)
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 annotation

Keywords - Biological processi

Purine biosynthesisUniRule annotation

Enzyme and pathway databases

BioCyciCKOS290338:GJ8L-1837-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
Ordered Locus Names:CKO_01840Imported
OrganismiCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)Imported
Taxonomic identifieri290338 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter
Proteomesi
  • UP000008148 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi290338.CKO_01840.

Structurei

3D structure databases

ProteinModelPortaliA8AHK4.
SMRiA8AHK4. Positions 1-456.
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

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
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.

A8AHK4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSSLTAVS PVDGRYGDKV SALRGIFSEY GLLKFRVQVE VRWLQKLAAH
60 70 80 90 100
AAIKEVPAFA ADANGFLDTI VANFNEEDAA RIKTIERTTN HDVKAVEYFL
110 120 130 140 150
KEKVADIPEL HAVSEFIHFA CTSEDINNLS HALMLKTARD EVILPYWRQL
160 170 180 190 200
IDAVKDLSVQ YRDIPLLSRT HGQPATPSTM GKEMANVAYR MERQFRQLNQ
210 220 230 240 250
VEILGKINGA VGNYNAHIAA YPEVDWHHFS EEFVTSLGIQ WNPYTTQIEP
260 270 280 290 300
HDYIAELFDC VARFNTILID FDRDVWGYIA LNHFKQRTIA GEIGSSTMPH
310 320 330 340 350
KVNPIDFENS EGNLGLANAV LQHLASKLPV SRWQRDLTDS TVLRNLGVGI
360 370 380 390 400
GYALIAYQST LKGVSKLEVN RDRLLDELDH NWEVLAEPIQ TVMRRYGIEK
410 420 430 440 450
PYEKLKELTR GKRVDAEGMK QFIDSLALPE EEKTRLKAMT PANYIGRAIT

MVDELK
Length:456
Mass (Da):51,716
Last modified:October 23, 2007 - v1
Checksum:i3020E6E8E61D3A32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000822 Genomic DNA. Translation: ABV12967.1.
RefSeqiWP_012132704.1. NC_009792.1.

Genome annotation databases

EnsemblBacteriaiABV12967; ABV12967; CKO_01840.
KEGGicko:CKO_01840.
PATRICi20386669. VBICitKos71230_1550.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000822 Genomic DNA. Translation: ABV12967.1.
RefSeqiWP_012132704.1. NC_009792.1.

3D structure databases

ProteinModelPortaliA8AHK4.
SMRiA8AHK4. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290338.CKO_01840.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV12967; ABV12967; CKO_01840.
KEGGicko:CKO_01840.
PATRICi20386669. VBICitKos71230_1550.

Phylogenomic databases

eggNOGiENOG4107QTF. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000252916.
KOiK01756.
OMAiTFGKEMA.
OrthoDBiEOG686NDB.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciCKOS290338:GJ8L-1837-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-895 / CDC 4225-83 / SGSC4696Imported.

Entry informationi

Entry nameiA8AHK4_CITK8
AccessioniPrimary (citable) accession number: A8AHK4
Entry historyi
Integrated into UniProtKB/TrEMBL: October 23, 2007
Last sequence update: October 23, 2007
Last modified: July 6, 2016
This is version 54 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.