Q9WUM5 (SUCA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Suclg1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	GTP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	succinate metabolic process Inferred from electronic annotation. Source: Compara succinyl-CoA metabolic process Inferred from electronic annotation. Source: Compara tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrial inner membrane Inferred from direct assay PubMed 12865426. Source: MGI plasma membrane Inferred from electronic annotation. Source: Compara succinate-CoA ligase complex (GDP-forming) Inferred from electronic annotation. Source: Compara
Molecular_function	ATP citrate synthase activity Inferred from electronic annotation. Source: InterPro GDP binding Inferred from electronic annotation. Source: Compara GTP binding Inferred from electronic annotation. Source: UniProtKB-KW cofactor binding Inferred from electronic annotation. Source: InterPro succinate-CoA ligase (ADP-forming) activity Inferred from electronic annotation. Source: EC succinate-CoA ligase (GDP-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 40	40	Mitochondrion By similarity
	Chain	41 – 346	306	Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial		PRO_0000033341
Sites
	Active site	299	1	Tele-phosphohistidine intermediate By similarity
Amino acid modifications
	Modified residue	54	1	N6-acetyllysine By similarity
	Cross-link	280		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5
Experimental info
	Sequence conflict	6	1	V → L in AAD33927. Ref.2
	Sequence conflict	175	1	V → I in BAC40634. Ref.1
	Sequence conflict	188	1	G → A in BAB22331. Ref.1
	Sequence conflict	201	1	R → K in AAD33927. Ref.2
	Sequence conflict	220	1	Q → H in AAD33927. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9WUM5 [UniParc]. Last modified February 10, 2009. Version 4. Checksum: 1EB7A444DFCE32FA	FASTA	346	36,155
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY. Tissue: Heart.
+	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.
IPI	IPI00406442.
RefSeq	NP_063932.2. NM_019879.3.
UniGene	Mm.29845.
3D structure databases
ProteinModelPortal	Q9WUM5.
SMR	Q9WUM5. Positions 42-346.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9WUM5. 1 interaction.
PTM databases
PhosphoSite	Q9WUM5.
Proteomic databases
PaxDb	Q9WUM5.
PRIDE	Q9WUM5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000064740; ENSMUSP00000065113; ENSMUSG00000052738.
GeneID	56451.
KEGG	mmu:56451.
UCSC	uc009cjm.2. mouse.
Organism-specific databases
CTD	8802.
MGI	MGI:1927234. Suclg1.
Phylogenomic databases
eggNOG	COG0074.
GeneTree	ENSGT00530000063275.
HOGENOM	HOG000239685.
HOVERGEN	HBG000957.
InParanoid	Q9WUM5.
KO	K01899.
OMA	KGRKKPM.
OrthoDB	EOG4WQ136.
Enzyme and pathway databases
UniPathway	UPA00223.
Gene expression databases
ArrayExpress	Q9WUM5.
Bgee	Q9WUM5.
CleanEx	MM_SUCLG1.
Genevestigator	Q9WUM5.
GermOnline	ENSMUSG00000052738. Mus musculus.
Family and domain databases
Gene3D	3.40.50.261. 1 hit. 3.40.50.720. 1 hit.
InterPro	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]
Pfam	PF02629. CoA_binding. 1 hit. PF00549. Ligase_CoA. 1 hit. [Graphical view]
PIRSF	PIRSF001553. SucCS_alpha. 1 hit.
PRINTS	PR01798. SCOASYNTHASE.
SMART	SM00881. CoA_binding. 1 hit. [Graphical view]
SUPFAM	SSF52210. CoA_ligase. 1 hit.
TIGRFAMs	TIGR01019. sucCoAalpha. 1 hit.
PROSITE	PS01216. SUCCINYL_COA_LIG_1. 1 hit. PS00399. SUCCINYL_COA_LIG_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SUCLG1. mouse.
NextBio	312668.
SOURCE	Search...

Entry information

Entry name

SUCA_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 125 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program