Q19842

PR
Gene name
pcca-1 (F27D9.5)
Protein name
Propionyl-CoA carboxylase alpha chain, mitochondrial
Names
PCCase subunit alpha, Propanoyl-CoA:carbon dioxide ligase subunit alpha
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_F27D9.5
EC number
6.4.1.3: Forming carbon-carbon bonds
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-60 (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 Q19842

Entry ID Method Resolution Chain Position Source
AF-Q19842-F1 Predicted AlphaFoldDB

No variants for Q19842

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q19842

No associated diseases with Q19842

8 regional properties for Q19842

Type Name Position InterPro Accession
domain Biotin/lipoyl attachment 649 - 724 IPR000089
binding_site Biotin-binding site 680 - 697 IPR001882
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 162 - 370 IPR005479
domain Biotin carboxylase-like, N-terminal domain 49 - 157 IPR005481
domain Biotin carboxylase, C-terminal 383 - 491 IPR005482
domain ATP-grasp fold 167 - 364 IPR011761
domain Biotin carboxylation domain 48 - 495 IPR011764
domain Propionyl-coenzyme A carboxylase, BT domain 512 - 649 IPR041265

Functions

Description
EC Number 6.4.1.3 Forming carbon-carbon bonds
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
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.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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.

1 GO annotations of biological process

Name Definition
lipid catabolic process The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P14882 Pcca Propionyl-CoA carboxylase alpha chain, mitochondrial Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MLRAASSIRA VANRGLATAA VARPGVPLDE REGKEIYTTV GIDYNEPKFD KILIANRGEI
70 80 90 100 110 120
ACRVIKTARA MGIKTVAVHS DVDSNSLHVK MADEAVCVGE APTAKSYLRA DRILQAVEDT
130 140 150 160 170 180
GAQAVHPGYG FLSENTKFAA ELEKAGAKFI GPNSKAILDM GDKIHSKKIA TAARVSMIPG
190 200 210 220 230 240
YDGEIADEDM CVKVSRDIGY PVMIKASAGG GGKGMRVAWN DKQAREGYRL SKQEAASSFG
250 260 270 280 290 300
DDRMLVEKFI DNPRHIEMQV LCDKHGNALW LNERECSIQR RNQKVIEEAP SSFVPPEMRR
310 320 330 340 350 360
KMGEQAVQLA KAVGYDSAGT VEFLVDSQRN FYFLEMNTRL QVEHPITECI TGIDIVQQML
370 380 390 400 410 420
RVSYGHPLPI TQEQVPLNGW AFESRVYAED PYKGFGLPSV GRLSRYVEPK HVDGVRCDSG
430 440 450 460 470 480
IREGSEISIY YDPLICKLVT HGDNREQALN RMQEALDNYV IRGVTHNIPL LRDIVQEKRF
490 500 510 520 530 540
RTGDITTKYL PEVYPEGFQG TSLSPKEQDV VIAFASALNA RKLARANQFL NQNKQRSTHV
550 560 570 580 590 600
ASFSKTYKFV SSLPVKEGER PTEHAVEVEF VEGSANKAQV RIGGKTVTIS GDLNLSHPVN
610 620 630 640 650 660
SIEVDGEHIT TQIVGKRAGE ITVLYKGTPF KVKVLPEQAV KYLQYMKEKA KVDLSTVVLS
670 680 690 700 710 720
PMPGAIKNVN VKPGDMVSEG QELVVMEAMK MQNSLHAGKT GRVKAVNVKV GATVDEGEVL
VELE