ID A0A026WVM4_OOCBI Unreviewed; 541 AA. AC A0A026WVM4; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 02-JUN-2021, entry version 28. 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}; GN ORFNames=X777_13892 {ECO:0000313|EMBL:EZA60067.1}; OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea; OC Formicidae; Dorylinae; Ooceraea. OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA60067.1, ECO:0000313|Proteomes:UP000053097}; RN [1] {ECO:0000313|EMBL:EZA60067.1, ECO:0000313|Proteomes:UP000053097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018; RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H., RA Zhang G., Kronauer D.J.; RT "The genome of the clonal raider ant Cerapachys biroi."; RL Curr. Biol. 24:451-458(2014). 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 --------------------------------------------------------------------------- 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; KK107083; EZA60067.1; -; Genomic_DNA. DR OMA; PSLYAMM; -. DR OrthoDB; 661265at2759; -. DR Proteomes; UP000053097; 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:UP000053097}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 7..232 FT /note="Thiolase_N" FT /evidence="ECO:0000259|Pfam:PF00108" FT DOMAIN 275..369 FT /note="Thiolase_C" FT /evidence="ECO:0000259|Pfam:PF02803" FT DOMAIN 433..526 FT /note="SCP2" FT /evidence="ECO:0000259|Pfam:PF02036" SQ SEQUENCE 541 AA; 58864 MW; 3352ED053F32BD4C CRC64; MVYKPKVYVI GVGMTKFEKP GRRDDFDYPQ MAKEAVSKAL QDSRIYYSNV DAVCVGYVYG DSTCGQRAVY EVGLSGCPIY NVNNNCSTGS TALYLGKQII ESGNAKCVLV LGFEKMERGS LMSKFMDRTN PMDKHVELMA DIAGITEGPI TAQMFGNAGL EHMKKYGTKP EHFAKIAYKN HLHSTNNPYS QFQEKYSLEQ IMNSPKIFGP LTKLQCCPTS DGAAAVVLAN EEFVRAHHLQ PQAVEVLAME MTTDQPATFT SLSCMNLVGY DMTRNAAEKV FTSTSFKPSD VDVVELHDCF SANELITYEA LGLCAPGHAG KMIDSGNNTY GGKYVINPSG GLISKGHPLG ATGLAQCAEL CWQLRGEAGM RQVPGAKLAL QHNIGLGGAV VVGLYRLGFP KQTGIMRHNV NVAADPSVFK ANVLFQTLAM AMEEDEEGLI DRVRGIYGFK VINGPGGAEG YWIVDAKTGK GKVEYNGKTK PDVTFTVSDT DVVDFISGKL NPQKAFFQGK VKIQGNMGLA LKLPDLQKRA AKKIEVLRAK L //