ID   SUCHY_RAT               Reviewed;         436 AA.
AC   Q68FU4; F1LXJ6;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Succinate--hydroxymethylglutarate CoA-transferase;
DE            EC=2.8.3.13;
DE   AltName: Full=SuccinylCoA:glutarate-CoA transferase;
DE   Flags: Precursor;
GN   Name=Sugct;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the succinyl-CoA-dependent conversion of glutarate
CC       to glutaryl-CoA. Can use different dicarboxylic acids as CoA acceptors,
CC       the preferred ones are glutarate, succinate, adipate, and 3-
CC       hydroxymethylglutarate (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-3-methylglutarate + succinyl-CoA = (3S)-hydroxy-3-
CC         methylglutaryl-CoA + succinate; Xref=Rhea:RHEA:12284,
CC         ChEBI:CHEBI:17325, ChEBI:CHEBI:30031, ChEBI:CHEBI:43074,
CC         ChEBI:CHEBI:57292; EC=2.8.3.13;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR   EMBL; AABR06091768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06091798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC079348; AAH79348.1; -; mRNA.
DR   RefSeq; NP_001014168.1; NM_001014146.1.
DR   AlphaFoldDB; Q68FU4; -.
DR   SMR; Q68FU4; -.
DR   STRING; 10116.ENSRNOP00000039228; -.
DR   iPTMnet; Q68FU4; -.
DR   PhosphoSitePlus; Q68FU4; -.
DR   PRIDE; Q68FU4; -.
DR   Ensembl; ENSRNOT00000108763; ENSRNOP00000079174; ENSRNOG00000066247.
DR   GeneID; 361253; -.
DR   KEGG; rno:361253; -.
DR   UCSC; RGD:1308114; rat.
DR   CTD; 79783; -.
DR   RGD; 1308114; Sugct.
DR   eggNOG; KOG3957; Eukaryota.
DR   GeneTree; ENSGT00940000157866; -.
DR   InParanoid; Q68FU4; -.
DR   OrthoDB; 983223at2759; -.
DR   PhylomeDB; Q68FU4; -.
DR   TreeFam; TF314188; -.
DR   PRO; PR:Q68FU4; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0047369; F:succinate-hydroxymethylglutarate CoA-transferase activity; ISS:UniProtKB.
DR   Gene3D; 3.30.1540.10; -; 1.
DR   Gene3D; 3.40.50.10540; -; 1.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Mitochondrion; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..8
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           9..436
FT                   /note="Succinate--hydroxymethylglutarate CoA-transferase"
FT                   /id="PRO_0000194728"
FT   ACT_SITE        203
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         392
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TNE1"
SQ   SEQUENCE   436 AA;  47549 MW;  4A3AAC53D121051B CRC64;
     MLRMLARAVA FRRSGRGQAG GRGLWTGRPQ SDCDSMKPLE GVRILDLTRV LAGPFATMNL
     GDLGAEVIKV ERPGAGDDTR SWGPPFVNTE STYFLSVNRN KKSIAVNIKD PRGVRIVKEL
     AAICDVFVEN YVPGKLSEMG LGYADIDKIA PHIVYCSITG YGQTGPMSHR AGYDAIASAM
     SGLMHITGPE DGDPVRPGVA MTDLATGLFA YGAIMAGLIQ RYRTGKGLFI DCNLLSSQVA
     CLTQVAANYL IGQKEAKRWG TAHGSIVPYQ AFKTKDGYLV IGAGNNQQFA VLCKILNLPE
     LIDDSKYRTN HLRVQNRKEL VKILSARFAE EVTAKWLCLF EGSGIPYGPI NSLKDVFSEA
     QVLHNGLVME MNHPTVGKIS VPGPAVRYSK FKMSEAKPPP LLGQHTRHIL KEVLRYDEGV
     IGELLCSGVI EQHETE