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

2 structures for Q01647

Entry ID Method Resolution Chain Position Source
3ZGB X-ray 271 A A/B 6-967 PDB
AF-Q01647-F1 Predicted AlphaFoldDB

No variants for Q01647

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q01647

No associated diseases with Q01647

2 regional properties for Q01647

Type Name Position InterPro Accession
active_site Phosphoenolpyruvate carboxylase, Lys active site 168 - 179 IPR018129
active_site Phosphoenolpyruvate carboxylase, His active site 592 - 604 IPR033129

Functions

Description
EC Number 4.1.1.31 Carboxy-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.

1 GO annotations of molecular function

Name Definition
phosphoenolpyruvate carboxylase activity Catalysis of the reaction: phosphate + oxaloacetate = phosphoenolpyruvate + HCO3-.

3 GO annotations of biological process

Name Definition
carbon fixation A metabolic process in which carbon (usually derived from carbon dioxide) is incorporated into organic compounds (usually carbohydrates).
photosynthesis The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide (CO2) using energy obtained from light rather than from the oxidation of chemical compounds.
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MANRNLEKLA SIDAQLRLLV PGKVSEDDKL IEYDALLLDK FLDILQDLHG EDLKEAVQEC
70 80 90 100 110 120
YELSAEYEGK HDPKKLEELG SVLTSLDPGD SIVIAKAFSH MLNLANLAEE VQIAYRRRIK
130 140 150 160 170 180
LKRGDFADEA NATTESDIEE TFKKLVLKLN KSPEEVFDAL KNQTVDLVLT AHPTQSVRRS
190 200 210 220 230 240
LLQKHGRIRN CLAQLYAKDI TPDDKQELDE ALHREIQAAF RTDEIRRTPP TPQDEMRAGM
250 260 270 280 290 300
SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG KHPRVTPEVT
310 320 330 340 350 360
RDVCLLARMM ASNMYFSQIE DLMFEMSMWR CNSELRVRAE ELYRTARRDV KHYIEFWKQV
370 380 390 400 410 420
PPTEPYRVIL GDVRDKLYNT RERSRHLLAH GISDIPEEAV YTNVEQFLEP LELCYRSLCD
430 440 450 460 470 480
CGDRVIADGS LLDFLRQVST FGLSLVKLDI RQESDRHTDV LDAITQHLEI GSYREWSEEK
490 500 510 520 530 540
RQEWLLAELS GKRPLFGSDL PKTEEVKDVL DTFNVLAELP SDCFGAYIIS MATSPSDVLA
550 560 570 580 590 600
VELLQRECHV KHPLRVVPLF EKLADLEAAP AAMARLFSID WYRNRIDGKQ EVMIGYSDSG
610 620 630 640 650 660
KDAGRFSAAW QLYKAQEEII KVAKEFGVKL VIFHGRGGTV GRGGGPTHLA ILSQPPDTIH
670 680 690 700 710 720
GSLRVTVQGE VIEQSFGEEH LCFRTLQRFC AATLEHGMNP PISPRPEWRE LMDQMAVVAT
730 740 750 760 770 780
EEYRSIVFKE PRFVEYFRLA TPELEYGRMN IGSRPSKRKP SGGIESLRAI PWIFAWTQTR
790 800 810 820 830 840
FHLPVWLGFG AAFKHAIKKD SKNLQMLQEM YKTWPFFRVT IDLVEMVFAK GDPGIAALND
850 860 870 880 890 900
KLLVSEDLWP FGESLRANYE ETKDYLLKIA GHRDLLEGDP YLKQRIRLRD SYITTLNVCQ
910 920 930 940 950 960
AYTLKRIRDP NYHVTLRPHI SKEYAAEPSK PADELIHLNP TSEYAPGLED TLILTMKGIA
AGMQNTG