ID A0A7L4ARC1_9CHAR Unreviewed; 502 AA. AC A0A7L4ARC1; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 29-SEP-2021, entry version 3. DE RecName: Full=Acetyl-CoA C-myristoyltransferase {ECO:0000256|ARBA:ARBA00024077}; DE EC=2.3.1.155 {ECO:0000256|ARBA:ARBA00024058}; DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073}; DE EC=2.3.1.176 {ECO:0000256|ARBA:ARBA00012352}; DE AltName: Full=Non-specific lipid-transfer protein {ECO:0000256|ARBA:ARBA00017183}; DE AltName: Full=Propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00017737}; DE AltName: Full=SCP-2/3-oxoacyl-CoA thiolase {ECO:0000256|ARBA:ARBA00024112}; DE AltName: Full=SCP-2/thiolase {ECO:0000256|ARBA:ARBA00024137}; DE AltName: Full=SCP-chi {ECO:0000256|ARBA:ARBA00017535}; DE AltName: Full=Sterol carrier protein 2 {ECO:0000256|ARBA:ARBA00014545}; DE AltName: Full=Sterol carrier protein X {ECO:0000256|ARBA:ARBA00014519}; DE Flags: Fragment; GN Name=Scp2 {ECO:0000313|EMBL:NXW28207.1}; GN ORFNames=PHASIM_R00346 {ECO:0000313|EMBL:NXW28207.1}; OS Phaetusa simplex (large-billed tern). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Charadriiformes; Laridae; Phaetusa. OX NCBI_TaxID=297813 {ECO:0000313|EMBL:NXW28207.1, ECO:0000313|Proteomes:UP000556165}; RN [1] {ECO:0000313|EMBL:NXW28207.1, ECO:0000313|Proteomes:UP000556165} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B10K-DU-009-16 {ECO:0000313|EMBL:NXW28207.1}; RC TISSUE=Muscle {ECO:0000313|EMBL:NXW28207.1}; RA Zhang G.; RT "Bird 10,000 Genomes (B10K) Project - Family phase."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=cholesta-5,7-dien-3beta-ol(in) = cholesta-5,7-dien-3beta- CC ol(out); Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759; CC Evidence={ECO:0000256|ARBA:ARBA00023986}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(9Z-octadecenoyl)-CoA + CoA = (7Z)-hexadecenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:47400, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:87695, ChEBI:CHEBI:87698; CC Evidence={ECO:0000256|ARBA:ARBA00023989}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47401; CC Evidence={ECO:0000256|ARBA:ARBA00023989}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxohexadecanedioyl-CoA + CoA = acetyl-CoA + CC tetradecanedioyl-CoA; Xref=Rhea:RHEA:40343, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:77081, ChEBI:CHEBI:77084; CC Evidence={ECO:0000256|ARBA:ARBA00023963}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344; CC Evidence={ECO:0000256|ARBA:ARBA00023963}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + butanoyl-CoA = 3-oxohexanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31111, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57371, ChEBI:CHEBI:62418; CC Evidence={ECO:0000256|ARBA:ARBA00023942}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113; CC Evidence={ECO:0000256|ARBA:ARBA00023942}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + decanoyl-CoA = 3-oxododecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:61430, ChEBI:CHEBI:62615; CC Evidence={ECO:0000256|ARBA:ARBA00023956}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185; CC Evidence={ECO:0000256|ARBA:ARBA00023956}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + dodecanoyl-CoA = 3-oxotetradecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31091, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57375, ChEBI:CHEBI:62543; CC Evidence={ECO:0000256|ARBA:ARBA00023957}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093; CC Evidence={ECO:0000256|ARBA:ARBA00023957}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + hexadecanoyl-CoA = 3-oxooctadecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:35279, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57379, ChEBI:CHEBI:71407; CC Evidence={ECO:0000256|ARBA:ARBA00023928}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281; CC Evidence={ECO:0000256|ARBA:ARBA00023928}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:62619, ChEBI:CHEBI:62620; CC Evidence={ECO:0000256|ARBA:ARBA00023960}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205; CC Evidence={ECO:0000256|ARBA:ARBA00023960}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + octanoyl-CoA = 3-oxodecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31087, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57386, ChEBI:CHEBI:62548; CC Evidence={ECO:0000256|ARBA:ARBA00024001}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089; CC Evidence={ECO:0000256|ARBA:ARBA00024001}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:18161, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57385; EC=2.3.1.155; CC Evidence={ECO:0000256|ARBA:ARBA00023951}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163; CC Evidence={ECO:0000256|ARBA:ARBA00023951}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cholesta-5,7-dien-3beta-ol(in) = cholesta-5,7-dien-3beta- CC ol(out); Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759; CC Evidence={ECO:0000256|ARBA:ARBA00023966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha- CC trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA; CC Xref=Rhea:RHEA:16865, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, CC ChEBI:CHEBI:57392, ChEBI:CHEBI:58507; EC=2.3.1.176; CC Evidence={ECO:0000256|ARBA:ARBA00023938}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16867; CC Evidence={ECO:0000256|ARBA:ARBA00023938}; CC -!- CATALYTIC ACTIVITY: CC Reaction=propanoyl-CoA + tetradecanoyl-CoA = 3-oxo-2- CC methylhexadecanoyl-CoA + CoA; Xref=Rhea:RHEA:46344, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:57392, CC ChEBI:CHEBI:86042; Evidence={ECO:0000256|ARBA:ARBA00023934}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:46346; CC Evidence={ECO:0000256|ARBA:ARBA00023934}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Peroxisome CC {ECO:0000256|ARBA:ARBA00004275}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family. CC {ECO:0000256|RuleBase:RU003557}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NXW28207.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VZZW01000100; NXW28207.1; -; Genomic_DNA. DR Proteomes; UP000556165; Unassembled WGS sequence. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0050632; F:propionyl-CoA C2-trimethyltridecanoyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR Gene3D; 3.30.1050.10; -; 1. DR Gene3D; 3.40.47.10; -; 1. DR InterPro; IPR003033; SCP2_sterol-bd_dom. DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS. DR InterPro; IPR020617; Thiolase_C. DR InterPro; IPR020613; Thiolase_CS. DR InterPro; IPR020616; Thiolase_N. DR Pfam; PF02036; SCP2; 1. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR SUPFAM; SSF55718; SSF55718; 1. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|RuleBase:RU003557}; KW Lipid transport {ECO:0000256|ARBA:ARBA00023055}; KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}; KW Reference proteome {ECO:0000313|Proteomes:UP000556165}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 2..196 FT /note="Thiolase_N" FT /evidence="ECO:0000259|Pfam:PF00108" FT DOMAIN 241..332 FT /note="Thiolase_C" FT /evidence="ECO:0000259|Pfam:PF02803" FT DOMAIN 392..493 FT /note="SCP2" FT /evidence="ECO:0000259|Pfam:PF02036" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NXW28207.1" FT NON_TER 502 FT /evidence="ECO:0000313|EMBL:NXW28207.1" SQ SEQUENCE 502 AA; 53829 MW; D840EB332DBA70B7 CRC64; GQKALADAGI PYSAVQQACV GYVYGDSTCG QRAIYHGLGL TGIPIINVNN NCATGSTALF MARQLVEGGL ADCVLALGFE RMAKGSLASG FSDRTNPMDK HLEIMINKYG LASAPIAPQM FANAGKEHME KYGTNPEYFA KIAWKNHSHS TNNPYSQFQK EYTLDEVLHS RKIFDFLTVL QCCPTSNGAA AAILASETFV KRHKLQPKAV EILAQVMATD FPSTFEENSC MKMVGYDMTK KAAEKCFEKA GLKPTDVDVI ELHDCFSVNE FITYEALGLC PEGRACDLID RGDNTYGGKW VINPSGGLIS KGHPLGATGL AQCAELCWQL RGLAGRRQVP GAKVALQHNL GLGGAVVVTL YGMGFPGAAS TGRIAAVPLS AAVDGFKSHL VFKEIEKKLQ EEGEQFVKKI GGVFAFKIKD GPGGKEATWI VDVKNGKGSV AVNSDKKADC TITMADTDLL ALMTGKMNPQ TAFFQGKLKV SGNMGMAMKL QNLQLQPGKA KL //