Structure of PDB 5ncc Chain F

Receptor sequence
>5nccF (length=578) Species: 554065 (Chlorella variabilis) [Search protein sequence]
SASAVEDIRKVLSDSSSPVAGQKYDYILVGGGTAACVLANRLSADGSKRV
LVLEAGPDNTSRDVKIPAAITRLFRSPLDWNLFSELQEQLAERQIYMARG
RLLGGSSATNATLYHRGAAGDYDAWGVEGWSSEDVLSWFVQAETNADFGP
GAYHGSGGPMRVENPRYTNKQLHTAFFKAAEEVGLTPNSDFNDWSHDHAG
YGTFQVMQDKGTRADMYRQYLKPVLGRRNLQVLTGAAVTKVNIDGKAQAL
GVEFSTDGPTGERLSAELAPGGEVIMCAGAVHTPFLLKHSGVGPSAELKE
FGIPVVSNLAGVGQNLQDQPACLTAAPVKEKYDGIAISDHIGQIRKRAIA
SYLLGGRGGLTSTGCDRGAFVRTAGQALPDLQVRFVPGMALDPDGVSTYV
RFAKFQSQGLKWPSGITMQLIACRPQSTGSVGLKSADPFAPPKLSPGYLT
DKDGADLATLRKGIHWARDVARSSALSEYLDGELFPGSGVVSDDQIDEYI
RRSIHSSNAITGTCKMGNAGDSSSVVDNQLRVHGVEGLRVVDASVVPKIP
GGQTGAPVVMIAERAAALLTGKATIGAS
3D structure
PDB5ncc An algal photoenzyme converts fatty acids to hydrocarbons.
ChainF
Resolution3.12 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R414 L487 I488 S574 A576 G619 Q620
Catalytic site (residue number reindexed from 1) R347 L420 I421 S507 A509 G552 Q553
Enzyme Commision number 4.1.1.106: fatty acid photodecarboxylase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0008812 choline dehydrogenase activity
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
GO:0016829 lyase activity
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0019285 glycine betaine biosynthetic process from choline
Cellular Component
GO:0009507 chloroplast
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ncc, PDBe:5ncc, PDBj:5ncc
PDBsum5ncc
PubMed28860382
UniProtA0A248QE08|FAP_CHLVA Fatty acid photodecarboxylase, chloroplastic (Gene Name=FAP)

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