Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q80WS1

Entry ID Method Resolution Chain Position Source
AF-Q80WS1-F1 Predicted AlphaFoldDB

20 variants for Q80WS1

Variant ID(s) Position Change Description Diseaes Association Provenance
rs236747424 63 S>G No EVA
rs3388860730 74 V>M No EVA
rs3388858093 97 K>N No EVA
rs3396507519 112 C>* No EVA
rs3397321177 112 C>S No EVA
rs3397268385 112 C>S No EVA
rs3388851531 114 N>I No EVA
rs3388821558 116 F>L No EVA
rs3388852429 123 A>S No EVA
rs249422125 178 A>S No EVA
rs3388847316 209 V>E No EVA
rs3388858934 220 C>Y No EVA
rs3388858990 223 D>Y No EVA
rs264251152 238 M>L No EVA
rs3397457334 283 G>D No EVA
rs3397321149 284 F>Y No EVA
rs3397303320 285 I>N No EVA
rs228946578 339 A>T No EVA
rs261357872 340 A>V No EVA
rs3388836425 361 R>* No EVA

No associated diseases with Q80WS1

2 regional properties for Q80WS1

Type Name Position InterPro Accession
domain ATP-grasp fold 119 - 304 IPR011761
domain ATP-grasp fold, RimK-type 114 - 302 IPR013651

Functions

Description
EC Number 6.3.1.17 Acid--ammonia (or amine) ligases (amide synthases)
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
citrate-L-glutamate ligase activity Catalysis of the reaction: ATP + citrate + L-glutamate = ADP + phosphate + beta-citryl-L-glutamate.
ligase activity, forming carbon-nitrogen bonds Catalysis of the joining of two molecules, or two groups within a single molecule, via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate.
metal ion binding Binding to a metal ion.
N-acetyl-L-aspartate-L-glutamate ligase activity Catalysis of the reaction: ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetylaspartyl-glutamate.

1 GO annotations of biological process

Name Definition
protein modification process The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q0VCE9 RIMKLB Beta-citrylglutamate synthase B Bos taurus (Bovine) PR
Q8IXN7 RIMKLA N-acetylaspartylglutamate synthase A Homo sapiens (Human) PR
Q9ULI2 RIMKLB Beta-citrylglutamate synthase B Homo sapiens (Human) PR
Q6PFX8 Rimkla N-acetylaspartylglutamate synthase A Mus musculus (Mouse) PR
10 20 30 40 50 60
MCSSVTGKLW FLTDRRIRED YPQKEILRAL KAKCCEEELD FRAVVMDEMV LTVEQGNLGL
70 80 90 100 110 120
RISGELISAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC RLMNRPQAIL NCVNKFWTFQ
130 140 150 160 170 180
ELAGHGVPLP DTFSYGGHEN FAKMIDEAEV LEFPMVVKNT RGHRGKAVFL ARDKHHLADL
190 200 210 220 230 240
SHLIRHEAPY LFQKYIKESH GRDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS
250 260 270 280 290 300
LSEQGKQLAI QVSNILGTDV CGIDLLMKDD GSFCVCEANA NVGFIAFDKA CNLDVAGIIA
310 320 330 340 350 360
DYAASLLPAG RLTRRMSLLS VVSTASETSE PELGPPASAA VDNMSASSSS VDSDPESTTE
370 380
REMLTKLPGG LFNMNQLLAN EIKLLVE