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Q9WUM5 (SUCA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Suclg1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

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

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle.

Subunit structure

Heterodimer of an alpha and a beta subunit By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the succinate/malate CoA ligase alpha subunit family.

Sequence caution

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Mitochondrion By similarity
Chain41 – 346306Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial
PRO_0000033341

Sites

Active site2991Tele-phosphohistidine intermediate By similarity

Amino acid modifications

Modified residue541N6-acetyllysine Ref.7
Modified residue571N6-acetyllysine; alternate Ref.7
Modified residue571N6-succinyllysine; alternate Ref.6
Modified residue661N6-acetyllysine; alternate Ref.7
Modified residue661N6-succinyllysine; alternate Ref.6
Modified residue811N6-acetyllysine Ref.7
Modified residue941N6-acetyllysine Ref.7
Modified residue1051N6-acetyllysine Ref.7
Modified residue3381N6-succinyllysine Ref.6
Cross-link280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Experimental info

Sequence conflict61V → L in AAD33927. Ref.2
Sequence conflict1751V → I in BAC40634. Ref.1
Sequence conflict1881G → A in BAB22331. Ref.1
Sequence conflict2011R → K in AAD33927. Ref.2
Sequence conflict2201Q → H in AAD33927. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9WUM5 [UniParc].

Last modified February 10, 2009. Version 4.
Checksum: 1EB7A444DFCE32FA

FASTA34636,155
        10         20         30         40         50         60 
MTATVVAAAA TATMVSSSSG LAAARLLSRT FLLQQNGIRH GSYTASRKHI YIDKNTKIIC 

        70         80         90        100        110        120 
QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGQKHLGLPV FNTVKEAKEK TGATASVIYV 

       130        140        150        160        170        180 
PPPFAAAAIN EAIDAEIPLV VCITEGIPQQ DMVRVKHRLT RQGTTRLIGP NCPGVINPGE 

       190        200        210        220        230        240 
CKIGIMPGHI HKKGRIGIVS RSGTLTYEAV HQTTQVGLGQ SLCIGIGGDP FNGTDFIDCL 

       250        260        270        280        290        300 
EVFLNDPATE GIILIGEIGG HAEENAAAFL KEHNSGPKAK PVVSFIAGIT APPGRRMGHA 

       310        320        330        340 
GAIIAGGKGG AKEKISALQS AGVVVSMSPA QLGTTIYKEF EKRKML 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS20246.2.
RefSeqNP_063932.2. NM_019879.3.
UniGeneMm.29845.

3D structure databases

ProteinModelPortalQ9WUM5.
SMRQ9WUM5. Positions 42-346.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9WUM5. 4 interactions.
MINTMINT-1841915.

PTM databases

PhosphoSiteQ9WUM5.

Proteomic databases

MaxQBQ9WUM5.
PaxDbQ9WUM5.
PRIDEQ9WUM5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064740; ENSMUSP00000065113; ENSMUSG00000052738.
GeneID56451.
KEGGmmu:56451.
UCSCuc009cjm.2. mouse.

Organism-specific databases

CTD8802.
MGIMGI:1927234. Suclg1.

Phylogenomic databases

eggNOGCOG0074.
GeneTreeENSGT00530000063275.
HOGENOMHOG000239685.
HOVERGENHBG000957.
InParanoidQ9WUM5.
KOK01899.
OMAFEQDPQT.
OrthoDBEOG74BJSG.
PhylomeDBQ9WUM5.
TreeFamTF300666.

Enzyme and pathway databases

UniPathwayUPA00223.

Gene expression databases

ArrayExpressQ9WUM5.
BgeeQ9WUM5.
CleanExMM_SUCLG1.
GenevestigatorQ9WUM5.

Family and domain databases

Gene3D3.40.50.261. 1 hit.
3.40.50.720. 1 hit.
InterProIPR017440. 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]
PfamPF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFPIRSF001553. SucCS_alpha. 1 hit.
PRINTSPR01798. SCOASYNTHASE.
SMARTSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMSSF52210. SSF52210. 1 hit.
TIGRFAMsTIGR01019. sucCoAalpha. 1 hit.
PROSITEPS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSUCLG1. mouse.
NextBio312668.
PROQ9WUM5.
SOURCESearch...

Entry information

Entry nameSUCA_MOUSE
AccessionPrimary (citable) accession number: Q9WUM5
Secondary accession number(s): Q8C2C3, Q9DBA3, Q9DCI8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot