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Q9WUM5

- SUCA_MOUSE

UniProt

Q9WUM5 - SUCA_MOUSE

Protein

Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial

Gene

Suclg1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 4 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity By similarity.By similarity

    Catalytic activityi

    GTP + succinate + CoA = GDP + phosphate + succinyl-CoA.
    ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei299 – 2991Tele-phosphohistidine intermediateBy similarity

    GO - Molecular functioni

    1. ATP citrate synthase activity Source: InterPro
    2. cofactor binding Source: InterPro
    3. GDP binding Source: Ensembl
    4. GTP binding Source: UniProtKB-KW
    5. succinate-CoA ligase (ADP-forming) activity Source: UniProtKB-EC
    6. succinate-CoA ligase (GDP-forming) activity Source: UniProtKB-EC

    GO - Biological processi

    1. succinate metabolic process Source: Ensembl
    2. succinyl-CoA metabolic process Source: Ensembl
    3. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00223.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC:6.2.1.4, EC:6.2.1.5)
    Alternative name(s):
    Succinyl-CoA synthetase subunit alpha
    Short name:
    SCS-alpha
    Gene namesi
    Name:Suclg1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1927234. Suclg1.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: MGI
    2. mitochondrion Source: MGI
    3. plasma membrane Source: Ensembl
    4. succinate-CoA ligase complex (GDP-forming) Source: Ensembl

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4040MitochondrionBy similarityAdd
    BLAST
    Chaini41 – 346306Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrialPRO_0000033341Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 541N6-acetyllysine1 Publication
    Modified residuei57 – 571N6-acetyllysine; alternate1 Publication
    Modified residuei57 – 571N6-succinyllysine; alternate1 Publication
    Modified residuei66 – 661N6-acetyllysine; alternate1 Publication
    Modified residuei66 – 661N6-succinyllysine; alternate1 Publication
    Modified residuei81 – 811N6-acetyllysine1 Publication
    Modified residuei94 – 941N6-acetyllysine1 Publication
    Modified residuei105 – 1051N6-acetyllysine1 Publication
    Cross-linki280 – 280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei338 – 3381N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ9WUM5.
    PaxDbiQ9WUM5.
    PRIDEiQ9WUM5.

    PTM databases

    PhosphoSiteiQ9WUM5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9WUM5.
    BgeeiQ9WUM5.
    CleanExiMM_SUCLG1.
    GenevestigatoriQ9WUM5.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit.By similarity

    Protein-protein interaction databases

    IntActiQ9WUM5. 4 interactions.
    MINTiMINT-1841915.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WUM5.
    SMRiQ9WUM5. Positions 42-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0074.
    GeneTreeiENSGT00530000063275.
    HOGENOMiHOG000239685.
    HOVERGENiHBG000957.
    InParanoidiQ9WUM5.
    KOiK01899.
    OMAiFEQDPQT.
    OrthoDBiEOG74BJSG.
    PhylomeDBiQ9WUM5.
    TreeFamiTF300666.

    Family and domain databases

    Gene3Di3.40.50.261. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR017440. Cit_synth/succinyl-CoA_lig_AS.
    IPR003781. CoA-bd.
    IPR005810. CoA_lig_alpha.
    IPR005811. CoA_ligase.
    IPR016040. NAD(P)-bd_dom.
    IPR016102. Succinyl-CoA_synth-like.
    [Graphical view]
    PfamiPF02629. CoA_binding. 1 hit.
    PF00549. Ligase_CoA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001553. SucCS_alpha. 1 hit.
    PRINTSiPR01798. SCOASYNTHASE.
    SMARTiSM00881. CoA_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF52210. SSF52210. 1 hit.
    TIGRFAMsiTIGR01019. sucCoAalpha. 1 hit.
    PROSITEiPS01216. SUCCINYL_COA_LIG_1. 1 hit.
    PS00399. SUCCINYL_COA_LIG_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9WUM5-1 [UniParc]FASTAAdd to Basket

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    MTATVVAAAA TATMVSSSSG LAAARLLSRT FLLQQNGIRH GSYTASRKHI    50
    YIDKNTKIIC QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGQKHLGLPV 100
    FNTVKEAKEK TGATASVIYV PPPFAAAAIN EAIDAEIPLV VCITEGIPQQ 150
    DMVRVKHRLT RQGTTRLIGP NCPGVINPGE CKIGIMPGHI HKKGRIGIVS 200
    RSGTLTYEAV HQTTQVGLGQ SLCIGIGGDP FNGTDFIDCL EVFLNDPATE 250
    GIILIGEIGG HAEENAAAFL KEHNSGPKAK PVVSFIAGIT APPGRRMGHA 300
    GAIIAGGKGG AKEKISALQS AGVVVSMSPA QLGTTIYKEF EKRKML 346
    Length:346
    Mass (Da):36,155
    Last modified:February 10, 2009 - v4
    Checksum:i1EB7A444DFCE32FA
    GO

    Sequence cautioni

    The sequence AAD33927.2 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH11087.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB22331.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB23804.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAC40634.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61V → L in AAD33927. 1 PublicationCurated
    Sequence conflicti175 – 1751V → I in BAC40634. (PubMed:16141072)Curated
    Sequence conflicti188 – 1881G → A in BAB22331. (PubMed:16141072)Curated
    Sequence conflicti201 – 2011R → K in AAD33927. 1 PublicationCurated
    Sequence conflicti220 – 2201Q → H in AAD33927. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002754 mRNA. Translation: BAB22331.1. Different initiation.
    AK005080 mRNA. Translation: BAB23804.1. Different initiation.
    AK088888 mRNA. Translation: BAC40634.1. Different initiation.
    AF144101 mRNA. Translation: AAD33927.2. Different initiation.
    BC011087 mRNA. Translation: AAH11087.1. Different initiation.
    CCDSiCCDS20246.2.
    RefSeqiNP_063932.2. NM_019879.3.
    UniGeneiMm.29845.

    Genome annotation databases

    EnsembliENSMUST00000064740; ENSMUSP00000065113; ENSMUSG00000052738.
    GeneIDi56451.
    KEGGimmu:56451.
    UCSCiuc009cjm.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002754 mRNA. Translation: BAB22331.1 . Different initiation.
    AK005080 mRNA. Translation: BAB23804.1 . Different initiation.
    AK088888 mRNA. Translation: BAC40634.1 . Different initiation.
    AF144101 mRNA. Translation: AAD33927.2 . Different initiation.
    BC011087 mRNA. Translation: AAH11087.1 . Different initiation.
    CCDSi CCDS20246.2.
    RefSeqi NP_063932.2. NM_019879.3.
    UniGenei Mm.29845.

    3D structure databases

    ProteinModelPortali Q9WUM5.
    SMRi Q9WUM5. Positions 42-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9WUM5. 4 interactions.
    MINTi MINT-1841915.

    PTM databases

    PhosphoSitei Q9WUM5.

    Proteomic databases

    MaxQBi Q9WUM5.
    PaxDbi Q9WUM5.
    PRIDEi Q9WUM5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000064740 ; ENSMUSP00000065113 ; ENSMUSG00000052738 .
    GeneIDi 56451.
    KEGGi mmu:56451.
    UCSCi uc009cjm.2. mouse.

    Organism-specific databases

    CTDi 8802.
    MGIi MGI:1927234. Suclg1.

    Phylogenomic databases

    eggNOGi COG0074.
    GeneTreei ENSGT00530000063275.
    HOGENOMi HOG000239685.
    HOVERGENi HBG000957.
    InParanoidi Q9WUM5.
    KOi K01899.
    OMAi FEQDPQT.
    OrthoDBi EOG74BJSG.
    PhylomeDBi Q9WUM5.
    TreeFami TF300666.

    Enzyme and pathway databases

    UniPathwayi UPA00223 .

    Miscellaneous databases

    ChiTaRSi SUCLG1. mouse.
    NextBioi 312668.
    PROi Q9WUM5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9WUM5.
    Bgeei Q9WUM5.
    CleanExi MM_SUCLG1.
    Genevestigatori Q9WUM5.

    Family and domain databases

    Gene3Di 3.40.50.261. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR017440. Cit_synth/succinyl-CoA_lig_AS.
    IPR003781. CoA-bd.
    IPR005810. CoA_lig_alpha.
    IPR005811. CoA_ligase.
    IPR016040. NAD(P)-bd_dom.
    IPR016102. Succinyl-CoA_synth-like.
    [Graphical view ]
    Pfami PF02629. CoA_binding. 1 hit.
    PF00549. Ligase_CoA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001553. SucCS_alpha. 1 hit.
    PRINTSi PR01798. SCOASYNTHASE.
    SMARTi SM00881. CoA_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52210. SSF52210. 1 hit.
    TIGRFAMsi TIGR01019. sucCoAalpha. 1 hit.
    PROSITEi PS01216. SUCCINYL_COA_LIG_1. 1 hit.
    PS00399. SUCCINYL_COA_LIG_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Cerebellum, Kidney and Thymus.
    2. "Sequence of the alpha subunit of succinyl-CoA synthetase in mouse."
      Tews K.N., Milavetz B.M., Lambeth D.O.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-346.
      Tissue: Heart.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-346.
    4. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 45-53; 58-92; 154-169 AND 279-295, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    5. "A proteomics approach to identify the ubiquitinated proteins in mouse heart."
      Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K., Choi H.W., Park Z.-Y., Yoo Y.J.
      Biochem. Biophys. Res. Commun. 357:731-736(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-280.
      Tissue: Heart.
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-66 AND LYS-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-57; LYS-66; LYS-81; LYS-94 AND LYS-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiSUCA_MOUSE
    AccessioniPrimary (citable) accession number: Q9WUM5
    Secondary accession number(s): Q8C2C3, Q9DBA3, Q9DCI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 136 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3