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 P14882

Entry ID Method Resolution Chain Position Source
AF-P14882-F1 Predicted AlphaFoldDB

No variants for P14882

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P14882

1 associated diseases with P14882

Without disease ID

8 regional properties for P14882

Type Name Position InterPro Accession
domain Biotin/lipoyl attachment 658 - 737 IPR000089
binding_site Biotin-binding site 693 - 710 IPR001882
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 185 - 393 IPR005479
domain Biotin carboxylase-like, N-terminal domain 72 - 180 IPR005481
domain Biotin carboxylase, C-terminal 406 - 514 IPR005482
domain ATP-grasp fold 190 - 387 IPR011761
domain Biotin carboxylation domain 71 - 518 IPR011764
domain Propionyl-coenzyme A carboxylase, BT domain 534 - 662 IPR041265

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
catalytic complex A protein complex which is capable of catalytic activity.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
metal ion binding Binding to a metal ion.
propionyl-CoA carboxylase activity Catalysis of the reaction: ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA.

2 GO annotations of biological process

Name Definition
cellular amino acid catabolic process The chemical reactions and pathways resulting in the breakdown of amino acids, organic acids containing one or more amino substituents.
fatty acid catabolic process The chemical reactions and pathways resulting in the breakdown of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q19842 pcca-1 Propionyl-CoA carboxylase alpha chain, mitochondrial Caenorhabditis elegans PR
10 20 30 40 50 60
MAGLWVRTVA LLAARRHWRR SSQQLLWTLK RAPRSSQQLL WTLKRAPVYS QQCLVVSRSL
70 80 90 100 110 120
SSVEYEPKEK TFDKILIANR GEIACRVIKT CRKMGIRTVA IHSDVDASSV HVKMADEAVC
130 140 150 160 170 180
VGPAPTSKSY LNMDAIMEAI KKTGAQAVHP GYGFLSENKE FAKCLAAEDV TFIGPDTHAI
190 200 210 220 230 240
QAMGDKIESK LLAKRAKVNT IPGFDGVLKD ADEAVRIARE IGYPVMIKAS AGGGGKGMRI
250 260 270 280 290 300
PWDDEETRDG FRFSSQEAAS SFGDDRLLIE KFIDNPRHIE IQVLGDKHGN ALWLNERECS
310 320 330 340 350 360
IQRRNQKVVE EAPSIFLDPE TRRAMGEQAV AWPKAVKYSS AGTVEFLVDS QKNFYFLEMN
370 380 390 400 410 420
TRLQVEHPVT ECITGLDLVQ EMILVAKGYP LRHKQEDIPI SGWAVECRVY AEDPYKSFGL
430 440 450 460 470 480
PSIGRLSQYQ EPIHLPGVRV DSGIQPGSDI SIYHDPMISK LVTYGSDRAE ALKRMEDALD
490 500 510 520 530 540
SYVIRGVTHN IPLLREVIIN TRFVKGDIST KFLSDVYPDG FKGHMLTPSE RDQLLAIASS
550 560 570 580 590 600
LFVASQLRAQ RFQEHSRVPV IRPDVAKWEL SVKLHDEDHT VVASNNGPTF NVEVDGSKLN
610 620 630 640 650 660
VTSTWNLASP LLSVNVDGTQ RTVQCLSPDA GGNMSIQFLG TVYKVHILTK LAAELNKFML
670 680 690 700 710 720
EKVPKDTSSV LRSPKPGVVV AVSVKPGDMV AEGQEICVIE AMKMQNSMTA GKMGKVKLVH
730
CKAGDTVGEG DLLVELE