Skip Header

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

Q9K4Z3

- ASSY_MORPR

UniProt

Q9K4Z3 - ASSY_MORPR

(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

Organism
Moritella profunda
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 sitei41 – 411ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
Binding sitei93 – 931CitrullineUniRule annotation
Binding sitei98 – 981CitrullineUniRule annotation
Binding sitei123 – 1231ATP; via amide nitrogenUniRule annotation
Binding sitei125 – 1251AspartateUniRule annotation
Binding sitei129 – 1291AspartateUniRule annotation
Binding sitei129 – 1291CitrullineUniRule annotation
Binding sitei130 – 1301AspartateUniRule annotation
Binding sitei133 – 1331CitrullineUniRule annotation
Binding sitei182 – 1821CitrullineUniRule annotation
Binding sitei191 – 1911CitrullineUniRule annotation
Binding sitei267 – 2671CitrullineUniRule annotation
Binding sitei279 – 2791CitrullineUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 219ATPUniRule 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

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
OrganismiMoritella profunda
Taxonomic identifieri111291 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesMoritellaceaeMoritella

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 – 404404Argininosuccinate synthasePRO_0000148613Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ9K4Z3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the argininosuccinate synthase family. Type 1 subfamily.UniRule annotation

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1.
InterProiIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR023434. Arginosuc_synth_type_1_subfam.
IPR024074. AS_cat/multimer_dom_body.
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.

Q9K4Z3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKMTQTVKKV VVAYSGGLDT SVILPWLQEN YDNCEIVAFV ADVGQGAEEL
60 70 80 90 100
EGIEAKALAS GASECYVVDL KDELVENYIY PTLKTGAVYE GTYLLGTSMA
110 120 130 140 150
RPIIAKAQVE IARKVGADAL CHGCTGKGND QIRFESCFAA LAPELTVIAP
160 170 180 190 200
WRIWDLTSRE SLLEYLAERD IPTAASATKI YSRDANAWHI SHEGGELEDP
210 220 230 240 250
WNQPSKQVWT MTVDPIDAPN EPEFLTISVV KGEITAVNGE AMSPYNTLMY
260 270 280 290 300
LNEKAAAHGV GRVDIVENRL VGMKSRGCYE TPGGTVMVEA LRGIEELVLD
310 320 330 340 350
KTTRKWKQTV AAEFSHLVYD GRWFTPLCAS LLAAAGTLAE EMNGEVIVKM
360 370 380 390 400
YKGSVQAIQK KSPNSLYSEE FATFGDDNVY DQSHAEGFIR LYSLSSRIKA

LASK
Length:404
Mass (Da):44,291
Last modified:October 1, 2000 - v1
Checksum:iEBE8AFBAB4E87F20
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ252020 Genomic DNA. Translation: CAB95017.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ252020 Genomic DNA. Translation: CAB95017.1 .

3D structure databases

ProteinModelPortali Q9K4Z3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00113 .

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPi MF_00005. Arg_succ_synth_type1.
InterProi IPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR023434. Arginosuc_synth_type_1_subfam.
IPR024074. AS_cat/multimer_dom_body.
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. "Evolution of arginine biosynthesis in the bacterial domain: novel gene-enzyme relationships from psychrophilic Moritella strains (Vibrionaceae) and evolutionary significance of N-alpha-acetyl ornithinase."
    Xu Y., Liang Z., Legrain C., Ruger H.J., Glansdorff N.
    J. Bacteriol. 182:1609-1615(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 2674.

Entry informationi

Entry nameiASSY_MORPR
AccessioniPrimary (citable) accession number: Q9K4Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3