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A9M4B1

- ASSY_NEIM0

UniProt

A9M4B1 - ASSY_NEIM0

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Protein

Argininosuccinate synthase

Gene

argG

Organism
Neisseria meningitidis serogroup C (strain 053442)
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 sitei46 – 461ATPUniRule annotation
Binding sitei102 – 1021CitrullineUniRule annotation
Binding sitei132 – 1321ATP; via amide nitrogenUniRule annotation
Binding sitei134 – 1341AspartateUniRule annotation
Binding sitei134 – 1341ATPUniRule annotation
Binding sitei138 – 1381AspartateUniRule annotation
Binding sitei138 – 1381CitrullineUniRule annotation
Binding sitei139 – 1391AspartateUniRule annotation
Binding sitei139 – 1391ATPUniRule annotation
Binding sitei142 – 1421CitrullineUniRule annotation
Binding sitei195 – 1951CitrullineUniRule annotation
Binding sitei197 – 1971ATPUniRule annotation
Binding sitei204 – 2041CitrullineUniRule annotation
Binding sitei206 – 2061CitrullineUniRule annotation
Binding sitei283 – 2831CitrullineUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289ATPUniRule annotation

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

BioCyciNMEN374833:GJ7Z-2089-MONOMER.
UniPathwayiUPA00068; UER00113.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate synthaseUniRule annotation (EC:6.3.4.5UniRule annotation)
Alternative name(s):
Citrulline--aspartate ligaseUniRule annotation
Gene namesi
Name:argGUniRule annotation
Ordered Locus Names:NMCC_2087
OrganismiNeisseria meningitidis serogroup C (strain 053442)
Taxonomic identifieri374833 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000001177: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Argininosuccinate synthasePRO_1000082403Add
BLAST

Proteomic databases

PRIDEiA9M4B1.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi374833.NMCC_2087.

Structurei

3D structure databases

ProteinModelPortaliA9M4B1.
SMRiA9M4B1. Positions 6-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the argininosuccinate synthase family. Type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0137.
HOGENOMiHOG000230094.
KOiK01940.
OMAiRIVEPIM.
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.

A9M4B1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQNHTILQS LPVGQKVGIA FSGGLDTSAA LLWMKLKGAL PYAYTANLGQ
60 70 80 90 100
PDEDDYNAIP KKAMEYGAEN ARLIDCRAQL AHEGIAAIQC GAFHVSTGGI
110 120 130 140 150
AYFNTTPLGR AVTGTMLVSA MKEDDVNIWG DGSTYKGNDI ERFYRYGLLT
160 170 180 190 200
NPALKIYKPW LDQQFIDELG GRHEMSEFLI ANGFNYKMSV EKAYSTDSNM
210 220 230 240 250
LGATHEAKDL EFLNSGIKIV KPIMGVAFWD ENVEVSPEEV SVRFEEGVPV
260 270 280 290 300
ALNGKEYADP VELFLEANRI GGRHGLGMSD QIENRIIEAK SRGIYEAPGM
310 320 330 340 350
ALFHIAYERL VTGIHNEDTI EQYRINGLRL GRLLYQGRWF DSQALMLRET
360 370 380 390 400
AQRWVAKAIT GEVTLELRRG NDYSILNTES PNLTYQPERL SMEKVEDAAF
410 420 430 440
TPLDRIGQLT MRNLDITDTR AKLGIYSQSG LLSLGEGSVL PQLGNKQ
Length:447
Mass (Da):49,650
Last modified:February 5, 2008 - v1
Checksum:i94FECD825352EA06
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000381 Genomic DNA. Translation: ABX74205.1.
RefSeqiWP_012222162.1. NC_010120.1.
YP_001600172.1. NC_010120.1.

Genome annotation databases

EnsemblBacteriaiABX74205; ABX74205; NMCC_2087.
GeneIDi5795435.
KEGGinmn:NMCC_2087.
PATRICi20349366. VBINeiMen117761_2568.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000381 Genomic DNA. Translation: ABX74205.1 .
RefSeqi WP_012222162.1. NC_010120.1.
YP_001600172.1. NC_010120.1.

3D structure databases

ProteinModelPortali A9M4B1.
SMRi A9M4B1. Positions 6-445.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 374833.NMCC_2087.

Proteomic databases

PRIDEi A9M4B1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX74205 ; ABX74205 ; NMCC_2087 .
GeneIDi 5795435.
KEGGi nmn:NMCC_2087.
PATRICi 20349366. VBINeiMen117761_2568.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00113 .
BioCyci NMEN374833:GJ7Z-2089-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. "Characterization of ST-4821 complex, a unique Neisseria meningitidis clone."
    Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z., Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z., Liang X., Xu J., Jin Q.
    Genomics 91:78-87(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 053442.

Entry informationi

Entry nameiASSY_NEIM0
AccessioniPrimary (citable) accession number: A9M4B1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: October 29, 2014
This is version 47 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