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NameSuccinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial
Synonyms
  • 6.2.1.5
  • ATP-specific succinyl-CoA synthetase subunit beta
  • Renal carcinoma antigen NY-REN-39
  • SCS-betaA
  • Succinyl-CoA synthetase beta-A chain
Gene NameSUCLA2
OrganismHuman
Amino acid sequence
>lcl|BSEQ0004436|Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMS
MELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVK
IVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGP
VLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENM
VKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDER
DKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEA
FKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALI
ADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
Number of residues463
Molecular Weight50316.88
Theoretical pI7.5
GO Classification
Functions
  • succinate-CoA ligase (ADP-forming) activity
  • ATP binding
  • metal ion binding
Processes
  • cellular metabolic process
  • succinate metabolic process
  • succinyl-CoA metabolic process
  • succinyl-CoA pathway
  • tricarboxylic acid cycle
  • small molecule metabolic process
Components
  • myelin sheath
  • mitochondrion
  • mitochondrial matrix
  • extracellular exosome
General FunctionSuccinate-coa ligase (adp-forming) activity
Specific FunctionCatalyzes the ATP-dependent ligation of succinate and CoA to form succinyl-CoA.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID7328935
UniProtKB IDQ9P2R7
UniProtKB Entry NameSUCB1_HUMAN
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0011628|Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2)
ATGGCGGCCTCCATGTTCTACGGCAGGCTAGTGGCCGTGGCCACCCTTCGGAACCACCGG
CCTCGGACGGCCCAGCGGGCTGCTGCTCAGGTTCTGGGAAGTTCTGGATTGTTTAATAAC
CATGGACTCCAAGTACAGCAGCAACAGCAAAGGAATCTCTCACTACATGAATACATGAGT
ATGGAATTATTGCAAGAAGCTGGTGTCTCCGTTCCCAAAGGATATGTGGCAAAGTCACCA
GATGAAGCTTATGCAATTGCCAAAAAATTAGGTTCAAAAGATGTCGTGATAAAGGCACAG
GTTTTAGCTGGTGGTAGAGGAAAAGGAACATTTGAAAGTGGCCTCAAAGGAGGAGTGAAG
ATAGTTTTCTCTCCAGAAGAAGCAAAAGCTGTTTCTTCACAAATGATTGGGAAAAAATTG
TTTACCAAGCAAACGGGAGAAAAGGGCAGAATATGCAATCAAGTATTGGTCTGTGAGCGA
AAATATCCCAGGAGAGAATACTACTTTGCAATAACAATGGAAAGGTCATTTCAAGGTCCT
GTATTAATAGGAAGTTCACATGGTGGTGTCAACATTGAAGATGTTGCTGCTGAGTCTCCT
GAAGCAATAATTAAAGAACCTATTGATATTGAAGAAGGCATCAAAAAGGAACAAGCTCTC
CAGCTTGCACAGAAGATGGGATTTCCACCTAATATTGTGGAATCAGCAGCAGAAAACATG
GTCAAGCTTTACAGCCTTTTTCTGAAATACGATGCAACCATGATAGAAATAAATCCAATG
GTGGAAGATTCAGATGGAGCTGTATTGTGTATGGATGCAAAGATCAATTTTGACTCTAAT
TCAGCCTATCGCCAAAAGAAAATCTTTGATCTACAGGACTGGACCCAGGAAGATGAAAGG
GACAAAGATGCTGCTAAGGCAAATCTCAACTACATTGGCCTCGATGGAAATATAGGCTGC
CTAGTAAATGGTGCTGGTTTGGCTATGGCCACAATGGATATAATAAAACTTCATGGAGGG
ACTCCAGCCAACTTCCTTGATGTTGGTGGTGGTGCTACAGTCCATCAAGTAACAGAAGCA
TTTAAGCTTATCACTTCAGATAAAAAGGTACTGGCTATTCTGGTCAACATTTTTGGAGGA
ATCATGCGCTGTGATGTTATTGCACAGGGTATAGTCATGGCAGTAAAAGACTTGGAAATT
AAAATACCTGTTGTGGTACGGTTACAAGGTACACGAGTCGATGATGCTAAGGCACTGATA
GCGGACAGTGGACTTAAAATACTTGCTTGTGATGACTTGGATGAAGCTGCTAGAATGGTT
GTAAAGCTCTCTGAAATAGTGACCTTAGCGAAGCAAGCACATGTGGATGTGAAATTTCAG
TTGCCAATATGA
GenBank Gene IDAB035863
GeneCard IDNot Available
GenAtlas IDSUCLA2
HGNC IDHGNC:11448
Chromosome Location13
Locus13q12.2-q13.3
References
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  16. Jaberi E, Chitsazian F, Ali Shahidi G, Rohani M, Sina F, Safari I, Malakouti Nejad M, Houshmand M, Klotzle B, Elahi E: The novel mutation p.Asp251Asn in the beta-subunit of succinate-CoA ligase causes encephalomyopathy and elevated succinylcarnitine. J Hum Genet. 2013 Aug;58(8):526-30. doi: 10.1038/jhg.2013.45. Epub 2013 Jun 13. 23759946