Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P13086

- SUCA_RAT

UniProt

P13086 - SUCA_RAT

Protein

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

Gene

Suclg1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (10 Feb 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 intermediate1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. succinate metabolic process Source: RGD
    2. succinyl-CoA metabolic process Source: RGD
    3. tricarboxylic acid cycle Source: RGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_216424. Citric acid cycle (TCA cycle).
    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 4

    Organism-specific databases

    RGDi619821. Suclg1.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4040MitochondrionAdd
    BLAST
    Chaini41 – 346306Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrialPRO_0000033343Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiP13086.
    PRIDEiP13086.

    PTM databases

    PhosphoSiteiP13086.

    Expressioni

    Gene expression databases

    GenevestigatoriP13086.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit.

    Protein-protein interaction databases

    BioGridi250390. 1 interaction.
    IntActiP13086. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP13086.
    SMRiP13086. Positions 42-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0074.
    GeneTreeiENSGT00530000063275.
    HOGENOMiHOG000239685.
    HOVERGENiHBG000957.
    InParanoidiQ6P7S4.
    KOiK01899.
    OMAiQNGVRHC.
    OrthoDBiEOG74BJSG.
    PhylomeDBiP13086.
    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.

    P13086-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAAVVAAAA TATMVSGSSG LAAARLLSRT FLLQQNGIRH GSYTASRKNI    50
    YIDKNTKVIC QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGKKHLGLPV 100
    FNTVKEAKEK TGATASVIYV PPPFAAAAIN EAIDAEIPLV VCITEGIPQQ 150
    DMVRVKHKLT RQGKTRLIGP NCPGIINPGE CKIGIMPGHI HKKGRIGIVS 200
    RSGTLTYEAV HQTTQVGLGQ SLCIGIGGDP FNGTNFIDCL DVFLKDPATE 250
    GIVLIGEIGG HAEENAAEFL KEHNSGPKAK PVVSFIAGIT APPGRRMGHA 300
    GAIIAGGKGG AKEKISALQS AGVIVSMSPA QLGTCMYKEF EKRKML 346
    Length:346
    Mass (Da):36,148
    Last modified:February 10, 2009 - v2
    Checksum:i2DDFC746C11B5B0C
    GO

    Sequence cautioni

    The sequence AAA41233.1 differs from that shown. Reason: Chimeric cDNA.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531V → L in AAA41233. (PubMed:3422742)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC061537 mRNA. Translation: AAH61537.2.
    J03621 mRNA. Translation: AAA41233.1. Sequence problems.
    PIRiA28962. SYRTSA.
    RefSeqiNP_446204.2. NM_053752.2.
    UniGeneiRn.3766.

    Genome annotation databases

    EnsembliENSRNOT00000007624; ENSRNOP00000007624; ENSRNOG00000005587.
    GeneIDi114597.
    KEGGirno:114597.
    UCSCiRGD:619821. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC061537 mRNA. Translation: AAH61537.2 .
    J03621 mRNA. Translation: AAA41233.1 . Sequence problems.
    PIRi A28962. SYRTSA.
    RefSeqi NP_446204.2. NM_053752.2.
    UniGenei Rn.3766.

    3D structure databases

    ProteinModelPortali P13086.
    SMRi P13086. Positions 42-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 250390. 1 interaction.
    IntActi P13086. 1 interaction.

    PTM databases

    PhosphoSitei P13086.

    Proteomic databases

    PaxDbi P13086.
    PRIDEi P13086.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000007624 ; ENSRNOP00000007624 ; ENSRNOG00000005587 .
    GeneIDi 114597.
    KEGGi rno:114597.
    UCSCi RGD:619821. rat.

    Organism-specific databases

    CTDi 8802.
    RGDi 619821. Suclg1.

    Phylogenomic databases

    eggNOGi COG0074.
    GeneTreei ENSGT00530000063275.
    HOGENOMi HOG000239685.
    HOVERGENi HBG000957.
    InParanoidi Q6P7S4.
    KOi K01899.
    OMAi QNGVRHC.
    OrthoDBi EOG74BJSG.
    PhylomeDBi P13086.
    TreeFami TF300666.

    Enzyme and pathway databases

    UniPathwayi UPA00223 .
    Reactomei REACT_216424. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    NextBioi 618767.
    PROi P13086.

    Gene expression databases

    Genevestigatori P13086.

    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 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].
      Tissue: Pituitary.
    2. "Cloning and sequencing of the cytoplasmic precursor to the alpha subunit of rat liver mitochondrial succinyl-CoA synthetase."
      Henning W.D., Upton C., McFadden G., Majumdar R., Bridger W.A.
      Proc. Natl. Acad. Sci. U.S.A. 85:1432-1436(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-346.
      Tissue: Liver.

    Entry informationi

    Entry nameiSUCA_RAT
    AccessioniPrimary (citable) accession number: P13086
    Secondary accession number(s): Q6P7S4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3