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A2SK99

- ASSY_METPP

UniProt

A2SK99 - ASSY_METPP

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Protein

Argininosuccinate synthase

Gene
argG, Mpe_A3035
Organism
Methylibium petroleiphilum (strain PM1)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATP By similarity
Binding sitei99 – 991Citrulline By similarity
Binding sitei129 – 1291ATP; via amide nitrogen By similarity
Binding sitei131 – 1311Aspartate By similarity
Binding sitei131 – 1311ATP By similarity
Binding sitei135 – 1351Aspartate By similarity
Binding sitei135 – 1351Citrulline By similarity
Binding sitei136 – 1361Aspartate By similarity
Binding sitei136 – 1361ATP By similarity
Binding sitei139 – 1391Citrulline By similarity
Binding sitei192 – 1921Citrulline By similarity
Binding sitei194 – 1941ATP By similarity
Binding sitei201 – 2011Citrulline By similarity
Binding sitei203 – 2031Citrulline By similarity
Binding sitei280 – 2801Citrulline By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 259ATP By similarity

GO - Molecular functioni

  1. argininosuccinate synthase activity Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMPET420662:GHBE-3072-MONOMER.
UniPathwayiUPA00068; UER00113.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate synthase (EC:6.3.4.5)
Alternative name(s):
Citrulline--aspartate ligase
Gene namesi
Name:argG
Ordered Locus Names:Mpe_A3035
OrganismiMethylibium petroleiphilum (strain PM1)
Taxonomic identifieri420662 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium
ProteomesiUP000000366: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446Argininosuccinate synthaseUniRule annotationPRO_1000025432Add
BLAST

Proteomic databases

PRIDEiA2SK99.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi420662.Mpe_A3035.

Structurei

3D structure databases

ProteinModelPortaliA2SK99.
SMRiA2SK99. Positions 3-442.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230094.
KOiK01940.
OMAiRQEMSEF.
OrthoDBiEOG6K9QCV.

Family and domain databases

Gene3Di1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00581. Arg_succ_synth_type2.
InterProiIPR023437. Arg_succ_synth_type2_subfam.
IPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR024074. AS_cat/multimer_dom_body.
IPR024073. AS_multimer_C_tail.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2SK99-1 [UniParc]FASTAAdd to Basket

« Hide

MATILQHLPT GQKVGIAFSG GLDTSAALHW MKLKGALPYA YTAHLGQPDE    50
PDYDEIPRKA MQYGAEKARL IDCRAQLVAE GLAALQAGAF HISTAGVTYF 100
NTTPIGRAVT GTMLVAAMKE DDVHIWGDGS TFKGNDIERF YRYGLLTNPA 150
LKIYKPWLDQ TFIDELGGRA EMSAFMTQAG FGYKMSAEKA YSTDSNLLGA 200
THEAKDLEHL SSGIRIVNPI MGVAFWRDEV EVKREEVTVR FEEGRPVALN 250
GIEFADPVAL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL 300
HIAYERLVTG IHNEDTIEQY RDNGRKLGRL LYQGRWFDPQ AIMLRETAQR 350
WVARAVTGEV ALELRRGNDY SILDTRSPNL TYQPERLSME KVEDAPFSPA 400
DRIGQLTMRN LDIVDTRAKL GIYAKSGLLS LGSGAALARL QNDDPS 446
Length:446
Mass (Da):49,318
Last modified:March 6, 2007 - v1
Checksum:i0F225FF441E1E530
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000555 Genomic DNA. Translation: ABM95988.1.
RefSeqiWP_011830611.1. NC_008825.1.
YP_001022223.1. NC_008825.1.

Genome annotation databases

EnsemblBacteriaiABM95988; ABM95988; Mpe_A3035.
GeneIDi4784957.
KEGGimpt:Mpe_A3035.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000555 Genomic DNA. Translation: ABM95988.1 .
RefSeqi WP_011830611.1. NC_008825.1.
YP_001022223.1. NC_008825.1.

3D structure databases

ProteinModelPortali A2SK99.
SMRi A2SK99. Positions 3-442.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 420662.Mpe_A3035.

Proteomic databases

PRIDEi A2SK99.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM95988 ; ABM95988 ; Mpe_A3035 .
GeneIDi 4784957.
KEGGi mpt:Mpe_A3035.

Phylogenomic databases

eggNOGi COG0137.
HOGENOMi HOG000230094.
KOi K01940.
OMAi RQEMSEF.
OrthoDBi EOG6K9QCV.

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00113 .
BioCyci MPET420662:GHBE-3072-MONOMER.

Family and domain databases

Gene3Di 1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPi MF_00581. Arg_succ_synth_type2.
InterProi IPR023437. Arg_succ_synth_type2_subfam.
IPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR024074. AS_cat/multimer_dom_body.
IPR024073. AS_multimer_C_tail.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
Pfami PF00764. Arginosuc_synth. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00032. argG. 1 hit.
PROSITEi PS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
    Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
    J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PM1.

Entry informationi

Entry nameiASSY_METPP
AccessioniPrimary (citable) accession number: A2SK99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: September 3, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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