eF-site ID 1nm8-A PDB Code 1nm8 Chain A click to enlarge Title Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer Classification TRANSFERASE Compound Carnitine O-acetyltransferase Source null (CACP_HUMAN) Sequence A:  HHTDPLPRLPVPPLQQSLDHYLKALQPIVSEEEWAHTKQL VDEFQASGGVGERLQKGLERRARKTENWLSEWWLKTAYLQ YRQPVVIYSSPGVMLPKQDFVDLQGQLRFAAKLIEGVLDF KVMIDNETLPVEYLGGKPLCMNQYYQILSSCRVPGPKQDT VSNFSKTKKPPTHITVVHNYQFFELDVYHSDGTPLTADQI FVQLEKIWNSSLQTNKEPVGILTSNHRNSWAKAYNTLIKD KVNRDSVRSIQKSIFTVCLDATMPRVSEDVYRSHVAGQML HGGGSRLNSGNRWFDKTLQFIVAEDGSCGLVYEHAAAEGP PIVTLLDYVIEYTKKPELVRSPMVPLPMPKKLRFNITPEI KSDIEKAKQNLSIMIQDLDITVMVFHHFGKDFPKSEKLSP DAFIQMALQLAYYRIYGQACATYESASLRMFHLGRTDTIR SASMDSLTFVKAMDDSSVTEHQKVELLRKAVQAHRGYTDR AIRGEAFDRHLLGLKLQAIEDLVSTPDIFMDTSYAIAMHF HLSTSQVPAKTDCVMFFGPVVPDGYGVCYNPMEAHINFSL SAYNSCAETNAARLAHYLEKALLDMRALLQS Description Functional site 1) chain A residue 322 type ACT_SITE sequence H description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 2) chain A residue 398 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P47934 source Swiss-Prot : SWS_FT_FI2 3) chain A residue 402 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P47934 source Swiss-Prot : SWS_FT_FI2 4) chain A residue 435 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P47934 source Swiss-Prot : SWS_FT_FI2 5) chain A residue 483 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P47934 source Swiss-Prot : SWS_FT_FI2 6) chain A residue 534 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P47934 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 431 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15099582 source Swiss-Prot : SWS_FT_FI3 8) chain A residue 433 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15099582 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15099582 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 247 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 11) chain A residue 14-29 type prosite sequence LPRLPVPPLQQSLDHY description ACYLTRANSF_C_1 Acyltransferases ChoActase / COT / CPT family signature 1. LPrLPVPpLqQSLdhY source prosite : PS00439 12) chain A residue 300-327 type prosite sequence RWFDKTLQFIVAEDGSCGLVYEHAAAEG description ACYLTRANSF_C_2 Acyltransferases ChoActase / COT / CPT family signature 2. RWfDKtLqFIvaeDGscglvyEHaaaEG source prosite : PS00440 13) chain A residue 72 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P47934 source Swiss-Prot : SWS_FT_FI4 14) chain A residue 240 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P47934 source Swiss-Prot : SWS_FT_FI5

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