P21265

PR
Gene name
ADSL
Protein name
Adenylosuccinate lyase
Names
ADSL, ASL, Adenylosuccinase, ASase
Species
Gallus gallus (Chicken)
KEGG Pathway
gga:396540
EC number
4.3.2.2: Lyases acting on amides, amidines, etc
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-111 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P21265

Entry ID Method Resolution Chain Position Source
AF-P21265-F1 Predicted AlphaFoldDB

18 variants for P21265

Variant ID(s) Position Change Description Diseaes Association Provenance
rs733236846 130 N>T No Ensembl
rs735942777 140 I>T No Ensembl
rs732539807 147 A>S No Ensembl
rs739360740 149 T>I No Ensembl
rs735346542 150 H>P No Ensembl
rs740272693 152 D>A No Ensembl
rs738202920 155 T>P No Ensembl
rs736313302 175 L>W No Ensembl
rs733380004 239 V>A No Ensembl
rs735184291 326 Q>P No Ensembl
rs739943274 332 L>V No Ensembl
rs1059324335 348 T>M No Ensembl
rs736719341 377 E>G No Ensembl
rs736039413 392 K>E No Ensembl
rs736817040 399 D>A No Ensembl
rs10723050 469 A>V No Ensembl
rs733481414 472 P>S No Ensembl
rs741425755 477 M>I No Ensembl

No associated diseases with P21265

3 regional properties for P21265

Type Name Position InterPro Accession
domain Adenylosuccinate lyase C-terminal 378 - 462 IPR019468
conserved_site Fumarate lyase, conserved site 289 - 298 IPR020557
domain Fumarate lyase, N-terminal 101 - 309 IPR022761

Functions

Description
EC Number 4.3.2.2 Lyases acting on amides, amidines, etc
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.

3 GO annotations of molecular function

Name Definition
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity Catalysis of the reaction: (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
identical protein binding Binding to an identical protein or proteins.
N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Catalysis of the reaction: N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP.

5 GO annotations of biological process

Name Definition
'de novo' AMP biosynthetic process The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from inosine 5'-monophosphate (IMP).
'de novo' IMP biosynthetic process The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
'de novo' XMP biosynthetic process The chemical reactions and pathways resulting in the formation of XMP, xanthosine monophosphate, from simpler precursors.
AMP salvage The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from derivatives of it (either adenine, ADP or adenosine 3',5'-bisphosphate) without de novo synthesis.
GMP biosynthetic process The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q05911 ADE13 Adenylosuccinate lyase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P30566 ADSL Adenylosuccinate lyase Homo sapiens (Human) PR
P54822 Adsl Adenylosuccinate lyase Mus musculus (Mouse) PR
10 20 30 40 50 60
MATPCAEEDP LARYRSPLVS RYASAEMGFN FSERKKFGTW RRLWLYLAQA EKSLGLPITD
70 80 90 100 110 120
EQIKEMEANL DNIDFKMAAE EEKKLRHDVM AHVHTFAHCC PKAAAIIHLG ATSCYVGDNT
130 140 150 160 170 180
DLIVLRDGFN LLLPKLARVI SRLADFAETH ADLPTLGFTH YQPAQLTTVG KRCCLWIQDL
190 200 210 220 230 240
CMDLQNLERA RDDLRFRGVK GTTGTQASFL QLFEGDHSKV EELDRLVTAK AGFKRSYMVT
250 260 270 280 290 300
GQTYSRKVDI EVLSVLASLG ASVHKICTDI RLLANLKEIE EPFEKDQIGS SAMPYKRNPM
310 320 330 340 350 360
RSERCCSLAR HLMTLVLDPL QTASVQWFER TLDDSANRRV CLAEAFLTAD IILSTLQNIS
370 380 390 400 410 420
EGLVVYPKVI DRRIRQELPF MATENIIMAM VKAGGNRQDC HEKIRVLSQQ AAAVVKQEGG
430 440 450 460 470 480
DNDFIARVRA DPYFSPIHEH LDSLLDPSSF TGRAPQQVAK FLKEEVRPAL IPYQSMMGGK
IELTL