{"metadata":{"accession":"A0A6P5KHM7","id":"A0A6P5KHM7_PHACI","source_organism":{"taxId":"38626","scientificName":"Phascolarctos cinereus","fullName":"Phascolarctos cinereus (Koala)"},"name":"Serine palmitoyltransferase small subunit B","description":["Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core. Within the SPT complex, SPTSSB stimulates the catalytic activity and plays a role in substrate specificity. SPT complexes with this subunit showing a preference for longer acyl-CoAs. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference"],"length":84,"sequence":"MPLADMMNLRYVKDYFAWLYYQYTLISCCAVLEPWERSMFNTILLTIVGMVVYTAYVFIPIHIRLAWEFFSEIFGDQSTASVSN","proteome":"UP000515140","gene":"SPTSSB","go_terms":null,"protein_evidence":3,"source_database":"unreviewed","is_fragment":false,"in_alphafold":true,"in_bfvd":false,"ida_accession":"23b61e0842cf0cb55f7e7f68da666ccdbb4943b7","counters":{"domain_architectures":4302,"entries":3,"isoforms":0,"proteomes":1,"sets":0,"structures":0,"taxa":1,"dbEntries":{"panther":1,"pfam":1,"interpro":1},"proteome":1,"taxonomy":1,"similar_proteins":4302}}}