SCOT_DROME
ID SCOT_DROME Reviewed; 516 AA.
AC Q9W058; Q8IRG3;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial {ECO:0000305};
DE EC=2.8.3.5 {ECO:0000255|PIRNR:PIRNR000858, ECO:0000269|PubMed:24100554};
DE AltName: Full=3-oxoacid CoA-transferase {ECO:0000305};
DE Flags: Precursor;
GN Name=SCOT {ECO:0000303|PubMed:24100554};
GN ORFNames=CG1140 {ECO:0000312|FlyBase:FBgn0035298};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL13483.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL13483.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAL13483.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0007744|PDB:4KGB}
RP X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 34-516, FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, AND SUBUNIT.
RX PubMed=24100554; DOI=10.1107/s1744309113024986;
RA Zhang M., Xu H.Y., Wang Y.C., Shi Z.B., Zhang N.N.;
RT "Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila
RT melanogaster.";
RL Acta Crystallogr. F Struct. Biol. Commun. 69:1089-1093(2013).
CC -!- FUNCTION: Key enzyme for ketone body catabolism (PubMed:24100554).
CC Transfers the CoA moiety from succinate to acetoacetate
CC (PubMed:24100554). Formation of the enzyme-CoA intermediate proceeds
CC via an unstable anhydride species formed between the carboxylate groups
CC of the enzyme and substrate (By similarity).
CC {ECO:0000250|UniProtKB:Q29551, ECO:0000269|PubMed:24100554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate;
CC Xref=Rhea:RHEA:24564, ChEBI:CHEBI:30031, ChEBI:CHEBI:35973,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:90726; EC=2.8.3.5;
CC Evidence={ECO:0000255|PIRNR:PIRNR000858,
CC ECO:0000269|PubMed:24100554};
CC -!- PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA
CC from succinyl-CoA: step 1/1. {ECO:0000255|PIRNR:PIRNR000858,
CC ECO:0000269|PubMed:24100554}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24100554}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BYC2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0035298};
CC IsoId=Q9W058-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0035298};
CC IsoId=Q9W058-2; Sequence=VSP_058745;
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000305}.
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DR EMBL; AE014296; AAF47600.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11508.1; -; Genomic_DNA.
DR EMBL; AY058254; AAL13483.1; -; mRNA.
DR RefSeq; NP_647683.1; NM_139426.3. [Q9W058-1]
DR RefSeq; NP_728699.1; NM_167928.2. [Q9W058-2]
DR PDB; 4KGB; X-ray; 2.64 A; A/B=34-516.
DR PDBsum; 4KGB; -.
DR AlphaFoldDB; Q9W058; -.
DR SMR; Q9W058; -.
DR IntAct; Q9W058; 3.
DR STRING; 7227.FBpp0072723; -.
DR PaxDb; Q9W058; -.
DR PRIDE; Q9W058; -.
DR DNASU; 38261; -.
DR EnsemblMetazoa; FBtr0072843; FBpp0072722; FBgn0035298. [Q9W058-2]
DR EnsemblMetazoa; FBtr0072844; FBpp0072723; FBgn0035298. [Q9W058-1]
DR GeneID; 38261; -.
DR KEGG; dme:Dmel_CG1140; -.
DR UCSC; CG1140-RA; d. melanogaster. [Q9W058-1]
DR CTD; 38261; -.
DR FlyBase; FBgn0035298; SCOT.
DR VEuPathDB; VectorBase:FBgn0035298; -.
DR eggNOG; KOG3822; Eukaryota.
DR GeneTree; ENSGT00390000009130; -.
DR InParanoid; Q9W058; -.
DR OMA; GTDYNKR; -.
DR PhylomeDB; Q9W058; -.
DR BRENDA; 2.8.3.5; 1994.
DR Reactome; R-DME-77108; Utilization of Ketone Bodies.
DR UniPathway; UPA00929; UER00894.
DR BioGRID-ORCS; 38261; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38261; -.
DR PRO; PR:Q9W058; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035298; Expressed in adult Malpighian tubule (Drosophila) and 45 other tissues.
DR ExpressionAtlas; Q9W058; baseline and differential.
DR Genevisible; Q8IRG3; DM.
DR GO; GO:0005739; C:mitochondrion; ISS:FlyBase.
DR GO; GO:0008260; F:3-oxoacid CoA-transferase activity; IDA:FlyBase.
DR GO; GO:0008410; F:CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0046950; P:cellular ketone body metabolic process; ISS:FlyBase.
DR GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
DR DisProt; DP02828; -.
DR InterPro; IPR012792; 3-oxoacid_CoA-transf_A.
DR InterPro; IPR012791; 3-oxoacid_CoA-transf_B.
DR InterPro; IPR014388; 3-oxoacid_CoA-transferase.
DR InterPro; IPR004165; CoA_trans_fam_I.
DR InterPro; IPR004164; CoA_transf_AS.
DR InterPro; IPR004163; CoA_transf_BS.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR13707; PTHR13707; 1.
DR Pfam; PF01144; CoA_trans; 2.
DR PIRSF; PIRSF000858; SCOT-t; 1.
DR SMART; SM00882; CoA_trans; 2.
DR SUPFAM; SSF100950; SSF100950; 2.
DR TIGRFAMs; TIGR02429; pcaI_scoA_fam; 1.
DR TIGRFAMs; TIGR02428; pcaJ_scoB_fam; 1.
DR PROSITE; PS01273; COA_TRANSF_1; 1.
DR PROSITE; PS01274; COA_TRANSF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..516
FT /note="Succinyl-CoA:3-ketoacid-coenzyme A transferase,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000438776"
FT ACT_SITE 340
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000255|PIRNR:PIRNR000858"
FT VAR_SEQ 1..20
FT /note="MLCRLVGNRSLGARYTASIK -> MDGWLA (in isoform B)"
FT /id="VSP_058745"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:4KGB"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:4KGB"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 231..242
FT /evidence="ECO:0007829|PDB:4KGB"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:4KGB"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 432..436
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:4KGB"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 468..475
FT /evidence="ECO:0007829|PDB:4KGB"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:4KGB"
FT HELIX 491..496
FT /evidence="ECO:0007829|PDB:4KGB"
FT STRAND 503..510
FT /evidence="ECO:0007829|PDB:4KGB"
SQ SEQUENCE 516 AA; 54904 MW; 3B6E076055655D2E CRC64;
MLCRLVGNRS LGARYTASIK AIACYSTSGK QRNGKIYESA IDAVADVQDG AQILFGGFGI
CGIPEKMINA LKQKGVKNIT GVSNNGGVDD TGLGVLIKQK QVSKVIGSYV GENTELVRQY
LEGELAVELT PQGTLAEKIR AGGAGIPAFY TPTGYATLVQ EGGAPIKYSK DGKVEISSEK
KPVKEFNGKN YVMEESIFAD FAFVKAQKAD PLGNLVFNKA ARNFNAPMCR AAKITVAEVE
EIVPIGALSP DEIHVPGIYI NRIFKGTNYN KRVERLRITE PKDPSKPAPP PNPAQVLRER
IARRVALEFH DGMYANLGIG IPVLSSNYIP KGMNVMLQSE NGILGLGPFP TKDKVDPDLI
NAGKESVTVV PGASYFGSDD SFAMIRGGHV DITILGAMEV SATGDLANWM IPGKLVKGMG
GAMDLVAAPG TKVIITMEHN ARDGSPKILD TCSLPLTGKG VIDMIISEKA VFTVEKGVGL
TLIEVAEGYT VDDIIASTGA KFTVSPNLKK MGQIPV
