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 Q8VXG7

Entry ID Method Resolution Chain Position Source
AF-Q8VXG7-F1 Predicted AlphaFoldDB

No variants for Q8VXG7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8VXG7

No associated diseases with Q8VXG7

1 regional properties for Q8VXG7

Type Name Position InterPro Accession
active_site Phenylalanine/histidine ammonia-lyases, active site 185 - 201 IPR022313

Functions

Description
EC Number 4.3.1.25 Ammonia-lyases
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.

3 GO annotations of molecular function

Name Definition
ammonia-lyase activity Catalysis of the release of ammonia by the cleavage of a carbon-nitrogen bond or the reverse reaction with ammonia as a substrate.
phenylalanine ammonia-lyase activity Catalysis of the reaction: L-phenylalanine = NH(4)(+) + trans-cinnamate.
tyrosine ammonia-lyase activity Catalysis of the reaction: L-tyrosine = NH(4)(+) + trans-4-coumarate.

6 GO annotations of biological process

Name Definition
cinnamic acid biosynthetic process The chemical reactions and pathways resulting in the formation of cinnamic acid, 3-phenyl-2-propenoic acid.
L-phenylalanine catabolic process The chemical reactions and pathways resulting in the breakdown of phenylalanine, 2-amino-3-phenylpropanoic acid.
phenylpropanoid biosynthetic process The chemical reactions and pathways resulting in the formation of aromatic derivatives of trans-cinnamic acid.
protein arginylation The conjugation of arginine to the N-terminal aspartate or glutamate of a protein; required for the degradation of the protein via the ubiquitin pathway.
response to cycloheximide Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cycloheximide stimulus. Cycloheximide (actidione) is an antibiotic produced by some Streptomyces species which interferes with protein synthesis in eukaryotes.
response to gibberellin Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gibberellin stimulus.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P45735 PAL Phenylalanine ammonia-lyase Vitis vinifera (Grape) PR
P42357 HAL Histidine ammonia-lyase Homo sapiens (Human) PR
P35492 Hal Histidine ammonia-lyase Mus musculus (Mouse) PR
P31425 PAL-1 Phenylalanine ammonia-lyase 1 Solanum tuberosum (Potato) PR
P31426 PAL-2 Phenylalanine ammonia-lyase 2 Solanum tuberosum (Potato) PR
Q0DZE0 ZB8 Phenylalanine ammonia-lyase Oryza sativa subsp japonica (Rice) PR
P14717 PAL Phenylalanine ammonia-lyase Oryza sativa subsp japonica (Rice) PR
P26600 PAL5 Phenylalanine ammonia-lyase Solanum lycopersicum (Tomato) (Lycopersicon esculentum) PR
P35511 PAL Phenylalanine ammonia-lyase Solanum lycopersicum (Tomato) (Lycopersicon esculentum) PR
10 20 30 40 50 60
MAGNGAIVES DPLNWGAAAA ELAGSHLDEV KRMVAQARQP VVKIEGSTLR VGQVAAVASA
70 80 90 100 110 120
KDASGVAVEL DEEARPRVKA SSEWILDCIA HGGDIYGVTT GFGGTSHRRT KDGPALQVEL
130 140 150 160 170 180
LRHLNAGIFG TGSDGHTLPS EVTRAAMLVR INTLLQGYSG IRFEILEAIT KLLNTGVSPC
190 200 210 220 230 240
LPLRGTITAS GDLVPLSYIA GLITGRPNAQ AVTVDGRKVD AAEAFKIAGI EGGFFKLNPK
250 260 270 280 290 300
EGLAIVNGTS VGSALAATVM YDANVLAVLS EVLSAVFCEV MNGKPEYTDH LTHKLKHHPG
310 320 330 340 350 360
SIEAAAIMEH ILDGSSFMKQ AKKVNELDPL LKPKQDRYAL RTSPQWLGPQ IEVIRAATKS
370 380 390 400 410 420
IEREVNSVND NPVIDVHRGK ALHGGNFQGT PIGVSMDNAR LAIANIGKLM FAQFSELVNE
430 440 450 460 470 480
FYNNGLTSNL AGSRNPSLDY GFKGTEIAMA SYCSELQYLG NPITNHVQSA DEHNQDVNSL
490 500 510 520 530 540
GLVSARKTAE AIDILKLMSS TYIVALCQAV DLRHLEENIK ASVKNTVTQV AKKVLTMNPS
550 560 570 580 590 600
GELSSARFSE KELISAIDRE AVFTYAEDAA SASLPLMQKL RAVLVDHALS SGERGAGALR
610 620 630 640 650 660
VLQDHQVRGG APRGAAPGGG GRPRGVAEGT APVANRIADS RSFPLYRFVR EELGCVFLTG
670 680 690 700
ERLKSPGEEC NKVFVGISQG KLVDPMLECL KEWDGKPLPI NIK