Structure of PDB 1on9 Chain F

Receptor sequence
>1on9F (length=516) Species: 1744 (Propionibacterium freudenreichii) [Search protein sequence]
LASTMEGRVEQLAEQRQVIEAGGGERRVEKQHSQGKQTARERLNNLLDPH
SFDEVGAFRKHRTTLFGMDKAVVPADGVVTGRGTILGRPVHAASQDFTVM
GGSAGETQSTKVVETMEQALLTGTPFLFFYDSGGARIQEGIDSLSGYGKM
FFANVKLSGVVPQIAIIAGPCAGGASYSPALTDFIIMTKKAHMFITGPQV
IKSVTGEDVTADELGGAEAHMAISGNIHFVAEDDDAAELIAKKLLSFLPQ
NNTEEASFVNPNNDVSPNTELRDIVPIDGKKGYDVRDVIAKIVDWGDYLE
VKAGYATNLVTAFARVNGRSVGIVANQPSVMSGCLDINASDKAAEFVNFC
DSFNIPLVQLVDVPGFLPGVQQEYGGIIRHGAKMLYAYSEATVPKITVVL
RKAYGGSYLAMCNRDLGADAVYAWPSAEIAVMGAEGAANVIFRKEIKAAD
DPDAMRAEKIEEYQNAFNTPYVAAARGQVDDVIDPADTRRKIASALEMYA
TKRQTRPAKKHGNFPC
3D structure
PDB1on9 Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core
ChainF
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A143 G181 G182 F374 G414 S415
Catalytic site (residue number reindexed from 1) A135 G173 G174 F366 G406 S407
Enzyme Commision number 2.1.3.1: methylmalonyl-CoA carboxytransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MCA F R35 F105 M108 G109 S111 R27 F97 M100 G101 S103
Gene Ontology
Molecular Function
GO:0003989 acetyl-CoA carboxylase activity
GO:0004658 propionyl-CoA carboxylase activity
GO:0016740 transferase activity
GO:0016874 ligase activity
GO:0047154 methylmalonyl-CoA carboxytransferase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
Cellular Component
GO:0009317 acetyl-CoA carboxylase complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:1on9, PDBe:1on9, PDBj:1on9
PDBsum1on9
PubMed12743028
UniProtQ8GBW6|12S_PROFR Methylmalonyl-CoA carboxyltransferase 12S subunit

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