Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Argininosuccinate lyase

Gene

argH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2-(N(omega)-L-arginino)succinate = fumarate + L-arginine.UniRule annotation

Pathwayi: L-arginine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Ornithine carbamoyltransferase chain I (argI), Ornithine carbamoyltransferase chain F (argF)
  2. Argininosuccinate synthase (argG)
  3. Argininosuccinate lyase (argH)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

  • argininosuccinate lyase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:ARGSUCCINLYA-MONOMER.
ECOL316407:JW3932-MONOMER.
MetaCyc:ARGSUCCINLYA-MONOMER.
UniPathwayiUPA00068; UER00114.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate lyaseUniRule annotation (EC:4.3.2.1UniRule annotation)
Short name:
ASALUniRule annotation
Alternative name(s):
ArginosuccinaseUniRule annotation
Gene namesi
Name:argHUniRule annotation
Ordered Locus Names:b3960, JW3932
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11223. argH.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Argininosuccinate lyasePRO_0000137768Add
BLAST

Proteomic databases

EPDiP11447.
PaxDbiP11447.
PRIDEiP11447.

Interactioni

Protein-protein interaction databases

BioGridi4263466. 10 interactions.
DIPiDIP-9142N.
STRINGi511145.b3960.

Structurei

Secondary structure

1
457
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 207Combined sources
Helixi23 – 264Combined sources
Helixi27 – 293Combined sources
Helixi30 – 4617Combined sources
Helixi52 – 7120Combined sources
Helixi73 – 786Combined sources
Helixi84 – 9613Combined sources
Helixi97 – 1026Combined sources
Turni103 – 1064Combined sources
Helixi109 – 14436Combined sources
Turni145 – 1484Combined sources
Beta strandi150 – 1556Combined sources
Beta strandi158 – 1647Combined sources
Helixi165 – 19026Combined sources
Turni198 – 2014Combined sources
Helixi209 – 2168Combined sources
Beta strandi219 – 2213Combined sources
Helixi225 – 2306Combined sources
Helixi233 – 25927Combined sources
Turni262 – 2643Combined sources
Helixi271 – 2733Combined sources
Helixi287 – 2948Combined sources
Helixi296 – 31015Combined sources
Helixi319 – 3235Combined sources
Helixi324 – 34623Combined sources
Helixi353 – 3608Combined sources
Turni363 – 3664Combined sources
Helixi367 – 37610Combined sources
Helixi381 – 39818Combined sources
Helixi402 – 4043Combined sources
Helixi407 – 4104Combined sources
Turni411 – 4133Combined sources
Helixi421 – 4244Combined sources
Helixi427 – 4326Combined sources
Helixi442 – 45615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TJ7X-ray2.44A/B1-457[»]
ProteinModelPortaliP11447.
SMRiP11447. Positions 3-457.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11447.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CH7. Bacteria.
COG0165. LUCA.
HOGENOMiHOG000242744.
InParanoidiP11447.
KOiK01755.
OMAiAHHLMAY.
PhylomeDBiP11447.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00006. Arg_succ_lyase. 1 hit.
InterProiIPR029419. Arg_succ_lyase_C.
IPR009049. Argininosuccinate_lyase.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF3. PTHR11444:SF3. 1 hit.
PfamiPF14698. ASL_C2. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00838. argH. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11447-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALWGGRFTQ AADQRFKQFN DSLRFDYRLA EQDIVGSVAW SKALVTVGVL
60 70 80 90 100
TAEEQAQLEE ALNVLLEDVR ARPQQILESD AEDIHSWVEG KLIDKVGQLG
110 120 130 140 150
KKLHTGRSRN DQVATDLKLW CKDTVSELLT ANRQLQSALV ETAQNNQDAV
160 170 180 190 200
MPGYTHLQRA QPVTFAHWCL AYVEMLARDE SRLQDALKRL DVSPLGCGAL
210 220 230 240 250
AGTAYEIDRE QLAGWLGFAS ATRNSLDSVS DRDHVLELLS AAAIGMVHLS
260 270 280 290 300
RFAEDLIFFN TGEAGFVELS DRVTSGSSLM PQKKNPDALE LIRGKCGRVQ
310 320 330 340 350
GALTGMMMTL KGLPLAYNKD MQEDKEGLFD ALDTWLDCLH MAALVLDGIQ
360 370 380 390 400
VKRPRCQEAA QQGYANATEL ADYLVAKGVP FREAHHIVGE AVVEAIRQGK
410 420 430 440 450
PLEDLPLSEL QKFSQVIDED VYPILSLQSC LDKRAAKGGV SPQQVAQAIA

FAQARLG
Length:457
Mass (Da):50,318
Last modified:October 1, 1993 - v3
Checksum:i0109EF31675B9717
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281R → G in AAB59147 (PubMed:6292860).Curated
Sequence conflicti40 – 401W → R in AAB59147 (PubMed:6292860).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA. Translation: AAC43066.1.
U00096 Genomic DNA. Translation: AAC76942.1.
AP009048 Genomic DNA. Translation: BAE77351.1.
M21446 Genomic DNA. Translation: AAA23479.1.
J01590 Genomic DNA. Translation: AAB59147.1.
PIRiC65203.
RefSeqiNP_418395.1. NC_000913.3.
WP_001230087.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76942; AAC76942; b3960.
BAE77351; BAE77351; BAE77351.
GeneIDi948463.
KEGGiecj:JW3932.
eco:b3960.
PATRICi32123441. VBIEscCol129921_4081.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA. Translation: AAC43066.1.
U00096 Genomic DNA. Translation: AAC76942.1.
AP009048 Genomic DNA. Translation: BAE77351.1.
M21446 Genomic DNA. Translation: AAA23479.1.
J01590 Genomic DNA. Translation: AAB59147.1.
PIRiC65203.
RefSeqiNP_418395.1. NC_000913.3.
WP_001230087.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TJ7X-ray2.44A/B1-457[»]
ProteinModelPortaliP11447.
SMRiP11447. Positions 3-457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263466. 10 interactions.
DIPiDIP-9142N.
STRINGi511145.b3960.

Proteomic databases

EPDiP11447.
PaxDbiP11447.
PRIDEiP11447.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76942; AAC76942; b3960.
BAE77351; BAE77351; BAE77351.
GeneIDi948463.
KEGGiecj:JW3932.
eco:b3960.
PATRICi32123441. VBIEscCol129921_4081.

Organism-specific databases

EchoBASEiEB1205.
EcoGeneiEG11223. argH.

Phylogenomic databases

eggNOGiENOG4105CH7. Bacteria.
COG0165. LUCA.
HOGENOMiHOG000242744.
InParanoidiP11447.
KOiK01755.
OMAiAHHLMAY.
PhylomeDBiP11447.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00114.
BioCyciEcoCyc:ARGSUCCINLYA-MONOMER.
ECOL316407:JW3932-MONOMER.
MetaCyc:ARGSUCCINLYA-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP11447.
PROiP11447.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00006. Arg_succ_lyase. 1 hit.
InterProiIPR029419. Arg_succ_lyase_C.
IPR009049. Argininosuccinate_lyase.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF3. PTHR11444:SF3. 1 hit.
PfamiPF14698. ASL_C2. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00838. argH. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiARLY_ECOLI
AccessioniPrimary (citable) accession number: P11447
Secondary accession number(s): Q2M8Q5, Q47060
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1993
Last modified: September 7, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.