Succinyl-CoA ligase [ADP-forming] subunit beta (P0A836)

Identification
Name:Succinyl-CoA ligase [ADP-forming] subunit beta
Synonyms:
  • Succinyl-CoA synthetase subunit beta
  • SCS-beta
Gene Name:sucC
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Succinic acid ↔ 1.0ADP + 1.0Phosphate + 1.0Succinyl-CoA
ReactionCard
SMPDB Reactions:
1.0Succinyl-CoA+1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Succinyl-CoA + 1.0Adenosine diphosphate + 1.0Phosphate + 1.0Succinyl-CoA + 1.0ADP → 1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Succinic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Succinic acid ↔ 1.0ADP + 1.0Phosphate + 1.0Succinyl-CoA
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB02092Itaconic acidMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00254Succinic acidMetaboCard
ECMDB01022Succinyl-CoAMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
nucleoside binding
purine nucleoside binding
Process
metabolic process
Gene Properties
Blattner:b0728
Gene OrientationClockwise
Centisome Percentage:16.43
Left Sequence End762237
Right Sequence End763403
Gene Sequence:
>1167 bp
GTGAAACATCTGCATCGATTCTTTAGCAGTGATGCCTCGGGAGGCATTATTCTTATCATT
GCCGCTATCCTGGCGATGATTATGGCCAACAGCGGCGCAACCAGTGGATGGTATCACGAC
TTTCTGGAGACGCCGGTTCAGCTCCGGGTTGGTTCACTCGAAATCAACAAAAACATGCTG
TTATGGATAAATGACGCGCTGATGGCGGTATTTTTCCTGTTAGTCGGTCTGGAAGTTAAA
CGTGAACTGATGCAAGGATCGCTAGCCAGCTTACGCCAGGCCGCATTTCCAGTTATCGCC
GCTATTGGTGGGATGATTGTGCCGGCATTACTCTATCTGGCTTTTAACTATGCCGATCCG
ATTACCCGCGAAGGGTGGGCGATCCCGGCGGCTACTGACATTGCTTTTGCACTTGGTGTA
CTGGCGCTGTTGGGAAGTCGTGTTCCGTTAGCGCTGAAGATCTTTTTGATGGCTCTGGCT
ATTATCGACGATCTTGGGGCCATCATTATCATCGCATTGTTCTACACTAATGACTTATCG
ATGGCCTCTCTTGGCGTCGCGGCTGTAGCAATTGCGGTACTCGCGGTATTGAATCTGTGT
GGTGCACGCCGCACGGGCGTCTATATTCTTGTTGGCGTGGTGTTGTGGACTGCGGTGTTG
AAATCGGGGGTTCACGCAACTCTGGCGGGGGTAATTGTCGGCTTCTTTATTCCTTTGAAA
GAGAAGCATGGGCGTTCTCCAGCGAAGCGACTGGAGCATGTGTTGCACCCGTGGGTGGCG
TATCTGATTTTGCCGCTGTTTGCATTTGCTAATGCTGGCGTTTCACTGCAAGGCGTCACG
CTGGATGGCTTGACCTCCATTCTGCCATTGGGGATCATCGCTGGCTTGCTGATTGGCAAA
CCGCTGGGGATTAGTCTGTTCTGCTGGTTGGCGCTGCGTTTGAAACTGGCGCATCTGCCT
GAGGGAACGACTTATCAGCAAATTATGGTGGTGGGGATCCTGTGCGGTATCGGTTTTACT
ATGTCTATCTTTATTGCCAGCCTGGCCTTTGGTAGCGTAGATCCAGAACTGATTAACTGG
GCGAAACTCGGTATCCTGGTCGGTTCTATCTCTTCGGCGGTAATTGGATACAGCTGGTTA
CGCGTTCGTTTGCGTCCATCAGTTTGA
Protein Properties
Pfam Domain Function:
Protein Residues:388
Protein Molecular Weight:41392
Protein Theoretical pI:5
PDB File:1JKJ
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Succinyl-CoA ligase [ADP-forming] subunit beta
MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGV
KVVNSKEDIRAFAENWLGKRLVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRR
VVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQGRELAFKLGLEGKLVQQFTKI
FMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP
REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTE
AFKIILSDDKVKAVLVNIFGGIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKK
LADSGLNIIAAKGLTDAAQQVVAAVEGK
References
External Links:
ResourceLink
Uniprot ID:P0A836
Uniprot Name:SUCC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321905
PDB ID:1JKJ
Ecogene ID:EG10981
Ecocyc:EG10981
ColiBase:b0728
Kegg Gene:b0728
EchoBASE ID:EB0974
CCDB:SUCC_ECOLI
BacMap:16128703
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Buck, D., Spencer, M. E., Guest, J. R. (1985). "Primary structure of the succinyl-CoA synthetase of Escherichia coli." Biochemistry 24:6245-6252. Pubmed: 3002435
  • Fraser, M. E., James, M. N., Bridger, W. A., Wolodko, W. T. (1999). "A detailed structural description of Escherichia coli succinyl-CoA synthetase." J Mol Biol 285:1633-1653. Pubmed: 9917402
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Joyce, M. A., Fraser, M. E., James, M. N., Bridger, W. A., Wolodko, W. T. (2000). "ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography." Biochemistry 39:17-25. Pubmed: 10625475
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Wolodko, W. T., Fraser, M. E., James, M. N., Bridger, W. A. (1994). "The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution." J Biol Chem 269:10883-10890. Pubmed: 8144675