SubmitCancel

Skip Header

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

P59608

- ASSY_BURM1

UniProt

P59608 - ASSY_BURM1

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Argininosuccinate synthase

Gene
argG, Bmul_5014, BMULJ_03499
Organism
Burkholderia multivorans (strain ATCC 17616 / 249)
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; via amide nitrogen and carbonyl oxygen 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

BioCyciBMUL395019:GIYO-3497-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:Bmul_5014, BMULJ_03499
OrganismiBurkholderia multivorans (strain ATCC 17616 / 249)
Taxonomic identifieri395019 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
ProteomesiUP000007064: Chromosome 2, UP000008815: Chromosome 2

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 – 445445Argininosuccinate synthaseUniRule annotationPRO_0000148694Add
BLAST

Proteomic databases

PRIDEiP59608.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi395019.Bmul_5014.

Structurei

3D structure databases

ProteinModelPortaliP59608.
SMRiP59608. Positions 2-440.

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.

P59608-1 [UniParc]FASTAAdd to Basket

« Hide

MSTILESLPT GQKVGIAFSG GLDTSAALHW MKLKGAVPYA YTANLGQPDE    50
DDYDAIPKRA LEYGAAGARL IDCRAQLVAE GIAALQSGAF HITTAGVTYF 100
NTTPIGRAVT GTMLVAAMKE DGVNIWGDGS TYKGNDIERF YRYGLLVNPD 150
LKIYKPWLDQ TFIDELGGRA EMSEFMRQSG FAYKMSAEKA YSTDSNLLGA 200
THEAKDLESL ESGIKIVNPI MGVAFWRDDV KIAAEEVTVR FEAGQPVALN 250
GVEFKDQVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL 300
YIAYERLVTG IHNEDTIEQY RENGRRLGRL LYQGRWFDPQ AIMLRETAQR 350
WVARAITGEV KIELRRGNDY SILSTKSPNL TYQPERLSME KVASTFSPRD 400
RIGQLTMRNL DITDTRDKLR VYTQVGLLTP GEASALPQIK GDSGE 445
Length:445
Mass (Da):49,252
Last modified:April 23, 2003 - v1
Checksum:i67581060BC11267F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB091438 Genomic DNA. Translation: BAC65286.1.
CP000869 Genomic DNA. Translation: ABX18685.1.
AP009386 Genomic DNA. Translation: BAG45371.1.
RefSeqiYP_001584977.1. NC_010086.1.
YP_001947907.1. NC_010805.1.

Genome annotation databases

EnsemblBacteriaiABX18685; ABX18685; Bmul_5014.
BAG45371; BAG45371; BMULJ_03499.
GeneIDi5768979.
6360599.
KEGGibmj:BMULJ_03499.
bmu:Bmul_5014.
PATRICi19169038. VBIBurMul203716_4556.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB091438 Genomic DNA. Translation: BAC65286.1 .
CP000869 Genomic DNA. Translation: ABX18685.1 .
AP009386 Genomic DNA. Translation: BAG45371.1 .
RefSeqi YP_001584977.1. NC_010086.1.
YP_001947907.1. NC_010805.1.

3D structure databases

ProteinModelPortali P59608.
SMRi P59608. Positions 2-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 395019.Bmul_5014.

Proteomic databases

PRIDEi P59608.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX18685 ; ABX18685 ; Bmul_5014 .
BAG45371 ; BAG45371 ; BMULJ_03499 .
GeneIDi 5768979.
6360599.
KEGGi bmj:BMULJ_03499.
bmu:Bmul_5014.
PATRICi 19169038. VBIBurMul203716_4556.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00113 .
BioCyci BMUL395019:GIYO-3497-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

« Hide 'large scale' publications
  1. "Distribution and organization of auxotrophic genes on the multichromosomal genome of Burkholderia multivorans ATCC 17616."
    Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.
    J. Bacteriol. 185:3333-3343(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of chromosome 2 of Burkholderia multivorans ATCC 17616."
    Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17616 / 249.
  3. "Complete genome sequence of Burkholderia multivorans ATCC 17616."
    Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., Hattori M., Tsuda M.
    Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17616 / 249.

Entry informationi

Entry nameiASSY_BURM1
AccessioniPrimary (citable) accession number: P59608
Secondary accession number(s): A9APH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: May 14, 2014
This is version 82 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

Similar proteinsi