SUCB1_HUMAN
ID SUCB1_HUMAN Reviewed; 463 AA.
AC Q9P2R7; B2RDE7; O95194; Q5T9Q4; Q5T9Q6; Q9NV21; Q9NVP7;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03220};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03220, ECO:0000269|PubMed:15877282};
DE AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03220};
DE Short=A-SCS {ECO:0000255|HAMAP-Rule:MF_03220};
DE AltName: Full=Succinyl-CoA synthetase beta-A chain {ECO:0000255|HAMAP-Rule:MF_03220};
DE Short=SCS-betaA {ECO:0000255|HAMAP-Rule:MF_03220};
DE Flags: Precursor;
GN Name=SUCLA2 {ECO:0000255|HAMAP-Rule:MF_03220};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10727444; DOI=10.1172/jci6816;
RA Furuyama K., Shigeru S.;
RT "Interaction between succinyl CoA synthetase and the heme-biosynthetic
RT enzyme ALAS-E is disrupted in sideroblastic anemia.";
RL J. Clin. Invest. 105:757-764(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-199.
RC TISSUE=Placenta, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-199.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-463 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP VARIANT THR-199.
RC TISSUE=Liver;
RX PubMed=9765291; DOI=10.1074/jbc.273.42.27580;
RA Johnson J.D., Mehus J.G., Tews K., Milavetz B.I., Lambeth D.O.;
RT "Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA
RT synthetases in multicellular eucaryotes.";
RL J. Biol. Chem. 273:27580-27586(1998).
RN [7]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [8]
RP INTERACTION WITH ALAS2.
RX PubMed=14643893; DOI=10.1016/s1357-2725(03)00246-2;
RA Cox T.C., Sadlon T.J., Schwarz Q.P., Matthews C.S., Wise P.D., Cox L.L.,
RA Bottomley S.S., May B.K.;
RT "The major splice variant of human 5-aminolevulinate synthase-2 contributes
RT significantly to erythroid heme biosynthesis.";
RL Int. J. Biochem. Cell Biol. 36:281-295(2004).
RN [9]
RP INVOLVEMENT IN MTDPS5, CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15877282; DOI=10.1086/430843;
RA Elpeleg O., Miller C., Hershkovitz E., Bitner-Glindzicz M.,
RA Bondi-Rubinstein G., Rahman S., Pagnamenta A., Eshhar S., Saada A.;
RT "Deficiency of the ADP-forming succinyl-CoA synthase activity is associated
RT with encephalomyopathy and mitochondrial DNA depletion.";
RL Am. J. Hum. Genet. 76:1081-1086(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-84, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP INVOLVEMENT IN MTDPS5, AND SUBCELLULAR LOCATION.
RX PubMed=17287286; DOI=10.1093/brain/awl383;
RA Ostergaard E., Hansen F.J., Sorensen N., Duno M., Vissing J., Larsen P.L.,
RA Faeroe O., Thorgrimsson S., Wibrand F., Christensen E., Schwartz M.;
RT "Mitochondrial encephalomyopathy with elevated methylmalonic acid is caused
RT by SUCLA2 mutations.";
RL Brain 130:853-861(2007).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78 AND LYS-143, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP SUBCELLULAR LOCATION, CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS]
RP AFTER ASN-52, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP VARIANTS MTDPS5 ARG-118 AND CYS-284.
RX PubMed=17301081; DOI=10.1093/brain/awl389;
RA Carrozzo R., Dionisi-Vici C., Steuerwald U., Lucioli S., Deodato F.,
RA Di Giandomenico S., Bertini E., Franke B., Kluijtmans L.A., Meschini M.C.,
RA Rizzo C., Piemonte F., Rodenburg R., Santer R., Santorelli F.M.,
RA van Rooij A., Vermunt-de Koning D., Morava E., Wevers R.A.;
RT "SUCLA2 mutations are associated with mild methylmalonic aciduria, Leigh-
RT like encephalomyopathy, dystonia and deafness.";
RL Brain 130:862-874(2007).
RN [17]
RP VARIANT MTDPS5 ASN-251.
RX PubMed=23759946; DOI=10.1038/jhg.2013.45;
RA Jaberi E., Chitsazian F., Ali Shahidi G., Rohani M., Sina F., Safari I.,
RA Malakouti Nejad M., Houshmand M., Klotzle B., Elahi E.;
RT "The novel mutation p.Asp251Asn in the beta-subunit of succinate-CoA ligase
RT causes encephalomyopathy and elevated succinylcarnitine.";
RL J. Hum. Genet. 58:526-530(2013).
CC -!- FUNCTION: ATP-specific succinyl-CoA synthetase functions in the citric
CC acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC synthesis of ATP and thus represents the only step of substrate-level
CC phosphorylation in the TCA (PubMed:15877282). The beta subunit provides
CC nucleotide specificity of the enzyme and binds the substrate succinate,
CC while the binding sites for coenzyme A and phosphate are found in the
CC alpha subunit (By similarity). {ECO:0000255|HAMAP-Rule:MF_03220,
CC ECO:0000269|PubMed:15877282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03220, ECO:0000269|PubMed:15877282};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03220};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03220};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03220, ECO:0000305|PubMed:15877282}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit
CC determines specificity for ATP (By similarity). Interacts with ALAS2
CC (PubMed:14643893). {ECO:0000255|HAMAP-Rule:MF_03220,
CC ECO:0000269|PubMed:14643893}.
CC -!- INTERACTION:
CC Q9P2R7; Q6RW13-2: AGTRAP; NbExp=6; IntAct=EBI-2269898, EBI-11522760;
CC Q9P2R7; Q15041: ARL6IP1; NbExp=6; IntAct=EBI-2269898, EBI-714543;
CC Q9P2R7; Q96DZ9-2: CMTM5; NbExp=6; IntAct=EBI-2269898, EBI-11522780;
CC Q9P2R7; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-2269898, EBI-3918971;
CC Q9P2R7; P43364: MAGEA11; NbExp=3; IntAct=EBI-2269898, EBI-739552;
CC Q9P2R7; Q969L2: MAL2; NbExp=3; IntAct=EBI-2269898, EBI-944295;
CC Q9P2R7; Q96CV9: OPTN; NbExp=3; IntAct=EBI-2269898, EBI-748974;
CC Q9P2R7; Q15436: SEC23A; NbExp=3; IntAct=EBI-2269898, EBI-81088;
CC Q9P2R7; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-2269898, EBI-1044859;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03220,
CC ECO:0000269|PubMed:15877282, ECO:0000269|PubMed:17287286,
CC ECO:0000269|PubMed:25944712}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2R7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2R7-2; Sequence=VSP_006292;
CC -!- TISSUE SPECIFICITY: Widely expressed. Not expressed in liver and lung.
CC {ECO:0000269|PubMed:9765291}.
CC -!- DISEASE: Mitochondrial DNA depletion syndrome 5 (MTDPS5) [MIM:612073]:
CC A disorder due to mitochondrial dysfunction. It is characterized by
CC infantile onset of hypotonia, neurologic deterioration, a hyperkinetic-
CC dystonic movement disorder, external ophthalmoplegia, deafness,
CC variable renal tubular dysfunction, and mild methylmalonic aciduria in
CC some patients. {ECO:0000269|PubMed:15877282,
CC ECO:0000269|PubMed:17287286, ECO:0000269|PubMed:17301081,
CC ECO:0000269|PubMed:23759946}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. ATP-specific subunit beta subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03220}.
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DR EMBL; AB035863; BAA92873.1; -; mRNA.
DR EMBL; AK001458; BAA91703.1; -; mRNA.
DR EMBL; AK001847; BAA91939.1; -; mRNA.
DR EMBL; AK315513; BAG37894.1; -; mRNA.
DR EMBL; AL157369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08777.1; -; Genomic_DNA.
DR EMBL; BC027587; AAH27587.1; -; mRNA.
DR EMBL; AF058953; AAC64396.1; -; mRNA.
DR CCDS; CCDS9406.1; -. [Q9P2R7-1]
DR RefSeq; NP_003841.1; NM_003850.2. [Q9P2R7-1]
DR PDB; 6G4Q; X-ray; 2.59 A; B=52-463.
DR PDBsum; 6G4Q; -.
DR AlphaFoldDB; Q9P2R7; -.
DR SMR; Q9P2R7; -.
DR BioGRID; 114331; 167.
DR ComplexPortal; CPX-6176; Mitochondrial succinyl-CoA synthetase complex, ATP-specific variant.
DR CORUM; Q9P2R7; -.
DR IntAct; Q9P2R7; 55.
DR MINT; Q9P2R7; -.
DR STRING; 9606.ENSP00000367923; -.
DR ChEMBL; CHEMBL4105973; -.
DR DrugBank; DB00787; Acyclovir.
DR GlyGen; Q9P2R7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P2R7; -.
DR PhosphoSitePlus; Q9P2R7; -.
DR SwissPalm; Q9P2R7; -.
DR BioMuta; SUCLA2; -.
DR DMDM; 94730427; -.
DR EPD; Q9P2R7; -.
DR jPOST; Q9P2R7; -.
DR MassIVE; Q9P2R7; -.
DR MaxQB; Q9P2R7; -.
DR PaxDb; Q9P2R7; -.
DR PeptideAtlas; Q9P2R7; -.
DR PRIDE; Q9P2R7; -.
DR ProteomicsDB; 83885; -. [Q9P2R7-1]
DR ProteomicsDB; 83886; -. [Q9P2R7-2]
DR Antibodypedia; 23774; 135 antibodies from 27 providers.
DR DNASU; 8803; -.
DR Ensembl; ENST00000643584.1; ENSP00000494987.1; ENSG00000136143.16. [Q9P2R7-1]
DR Ensembl; ENST00000646932.1; ENSP00000494360.1; ENSG00000136143.16. [Q9P2R7-1]
DR GeneID; 8803; -.
DR KEGG; hsa:8803; -.
DR MANE-Select; ENST00000646932.1; ENSP00000494360.1; NM_003850.3; NP_003841.1.
DR UCSC; uc001vbs.3; human. [Q9P2R7-1]
DR CTD; 8803; -.
DR DisGeNET; 8803; -.
DR GeneCards; SUCLA2; -.
DR GeneReviews; SUCLA2; -.
DR HGNC; HGNC:11448; SUCLA2.
DR HPA; ENSG00000136143; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; SUCLA2; -.
DR MIM; 603921; gene.
DR MIM; 612073; phenotype.
DR neXtProt; NX_Q9P2R7; -.
DR OpenTargets; ENSG00000136143; -.
DR Orphanet; 1933; Mitochondrial DNA depletion syndrome, encephalomyopathic form with methylmalonic aciduria.
DR PharmGKB; PA36245; -.
DR VEuPathDB; HostDB:ENSG00000136143; -.
DR eggNOG; KOG2799; Eukaryota.
DR GeneTree; ENSGT00390000010170; -.
DR HOGENOM; CLU_037430_0_0_1; -.
DR InParanoid; Q9P2R7; -.
DR PhylomeDB; Q9P2R7; -.
DR TreeFam; TF300624; -.
DR BioCyc; MetaCyc:ENSG00000136143-MON; -.
DR BRENDA; 6.2.1.5; 2681.
DR PathwayCommons; Q9P2R7; -.
DR Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR SignaLink; Q9P2R7; -.
DR SIGNOR; Q9P2R7; -.
DR UniPathway; UPA00223; UER00999.
DR BioGRID-ORCS; 8803; 146 hits in 1075 CRISPR screens.
DR ChiTaRS; SUCLA2; human.
DR GeneWiki; SUCLA2; -.
DR GenomeRNAi; 8803; -.
DR Pharos; Q9P2R7; Tchem.
DR PRO; PR:Q9P2R7; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9P2R7; protein.
DR Bgee; ENSG00000136143; Expressed in jejunal mucosa and 210 other tissues.
DR ExpressionAtlas; Q9P2R7; baseline and differential.
DR Genevisible; Q9P2R7; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0042709; C:succinate-CoA ligase complex; IBA:GO_Central.
DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR GO; GO:0006105; P:succinate metabolic process; IEA:Ensembl.
DR GO; GO:1901289; P:succinyl-CoA catabolic process; IC:ComplexPortal.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006781; P:succinyl-CoA pathway; NAS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.261; -; 1.
DR HAMAP; MF_00558; Succ_CoA_beta; 1.
DR HAMAP; MF_03220; Succ_CoA_betaA_euk; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005811; CoA_ligase.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR034723; Succ_CoA_betaA_euk.
DR InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11815; PTHR11815; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
DR TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Disease variant; Ligase; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Primary mitochondrial disease;
KW Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 53..463
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT /id="PRO_0000033352"
FT DOMAIN 61..288
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 105..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 323
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT BINDING 380..382
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT SITE 94
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT SITE 162
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03220"
FT MOD_RES 78
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 84
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 88
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 88
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 129
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT MOD_RES 368
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I9"
FT VAR_SEQ 26..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_006292"
FT VARIANT 13
FT /note="V -> M (in dbSNP:rs35201084)"
FT /id="VAR_046214"
FT VARIANT 118
FT /note="G -> R (in MTDPS5; dbSNP:rs121908537)"
FT /evidence="ECO:0000269|PubMed:17301081"
FT /id="VAR_046215"
FT VARIANT 199
FT /note="S -> T (in dbSNP:rs7320366)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9765291, ECO:0000269|Ref.4"
FT /id="VAR_013459"
FT VARIANT 251
FT /note="D -> N (in MTDPS5; dbSNP:rs397515462)"
FT /evidence="ECO:0000269|PubMed:23759946"
FT /id="VAR_070123"
FT VARIANT 284
FT /note="R -> C (in MTDPS5; dbSNP:rs121908538)"
FT /evidence="ECO:0000269|PubMed:17301081"
FT /id="VAR_046216"
FT CONFLICT 40
FT /note="N -> D (in Ref. 2; BAA91939)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="I -> V (in Ref. 2; BAA91939)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="N -> S (in Ref. 2; BAA91703)"
FT /evidence="ECO:0000305"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:6G4Q"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6G4Q"
FT TURN 143..147
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:6G4Q"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:6G4Q"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 252..262
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 325..337
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 385..397
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 413..421
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:6G4Q"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:6G4Q"
FT HELIX 433..452
FT /evidence="ECO:0007829|PDB:6G4Q"
SQ SEQUENCE 463 AA; 50317 MW; 1E1651728AF3B5CD CRC64;
MAASMFYGRL VAVATLRNHR PRTAQRAAAQ VLGSSGLFNN HGLQVQQQQQ RNLSLHEYMS
MELLQEAGVS VPKGYVAKSP DEAYAIAKKL GSKDVVIKAQ VLAGGRGKGT FESGLKGGVK
IVFSPEEAKA VSSQMIGKKL FTKQTGEKGR ICNQVLVCER KYPRREYYFA ITMERSFQGP
VLIGSSHGGV NIEDVAAESP EAIIKEPIDI EEGIKKEQAL QLAQKMGFPP NIVESAAENM
VKLYSLFLKY DATMIEINPM VEDSDGAVLC MDAKINFDSN SAYRQKKIFD LQDWTQEDER
DKDAAKANLN YIGLDGNIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG GATVHQVTEA
FKLITSDKKV LAILVNIFGG IMRCDVIAQG IVMAVKDLEI KIPVVVRLQG TRVDDAKALI
ADSGLKILAC DDLDEAARMV VKLSEIVTLA KQAHVDVKFQ LPI
