| Identification |
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| Name: | Methylmalonyl-CoA decarboxylase |
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| Synonyms: | |
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| Gene Name: | mmcD |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in catalytic activity |
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| Specific Function: | (S)-methylmalonyl-CoA = propanoyl-CoA + CO(2) |
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| Cellular Location: | Not Available |
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| SMPDB Pathways: | |
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| KEGG Pathways: | |
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| KEGG Reactions: | |
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| SMPDB Reactions: | |
1.0 | + | 1.0 | → | 1.0 | + | 1.0Propionyl-CoA | + | 1.0 |
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1.0R-Methylmalonyl-CoA | + | 1.0 | → | 1.0 | + | 1.0 |
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| Complex Reactions: | |
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| Metabolites: | |
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| GO Classification: | | Function |
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| catalytic activity | | Process |
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| metabolic process |
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| Gene Properties |
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| Blattner: | b2919 |
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| Gene Orientation | Clockwise |
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| Centisome Percentage: | 66.00 |
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| Left Sequence End | 3062015 |
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| Right Sequence End | 3062800 |
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| Gene Sequence: | >786 bp
ATGAATTCAAAAAAGCTTTGTTGCATATGTGTGTTATTCTCGCTGCTTGCAGGATGTGCC
TCTGAATCTTCTATTGATGAAAAGAAGAAAAAAGCTCAAGTCACACAAAGTAATATTAAT
AAAAACACTCCCCAGCAACTGACAGACAAAGATTTATTCGGTAATGAAACCACTCTGGCC
GTATCCGAAGAGGATATTCAAGCTGCGCTTGATGGAGATGAGTTCCGCGTTCCCCTTAAT
TCTCCTGTAATACTTGTTCAATCCGGCAACCGCGCACCGGAAACCATTATGCAGGAGGAG
ATGCGAAAATATTATACTGTTTCCACATTCTCTGGTATCCCGGACAGGCAAAAGCCTCTG
ACTTGTAACAAAAACAAAGATAAAAATGAGAACGAGGATGTTGCCAGTGCTGAGAATATG
AACTGGATGCAGGCACTGCGTTTTGTGGCTGCAAAAGGACATCAGAAAGCGATTATTGTT
TACCAGGATATGTTGCAGACAGGAAAATATGACTCTGCGCTGAAATCAACAGTATGGTCC
GACTATAAAAATGACAAACTCACTGACGCTATCTCCCTGCGCTACCTGGTACGTTTCACG
CTGGTGGATGTGGCAACAGGTGAGTGGGCTACCTGGTCGCCGGTGAATTATGAATATAAA
GTGCTTCCACCATTGCCCGACAAGAATGAAGCCAGTACGACTGATATGACAGAGCAGCAA
ATCATGCAACTTAAGCAAAAGACCTATAAAGCGATGGTAAAAGATTTGGTTAACCGCTAT
CAATAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 261 |
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| Protein Molecular Weight: | 29172 |
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| Protein Theoretical pI: | 6 |
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| PDB File: | 1EF9 |
| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >Methylmalonyl-CoA decarboxylase
MSYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCIILRAPSGSK
VFSAGHDIHELPSGGRDPLSYDDPLRQITRMIQKFPKPIISMVEGSVWGGAFEMIMSSDL
IIAASTSTFSMTPVNLGVPYNLVGIHNLTRDAGFHIVKELIFTASPITAQRALAVGILNH
VVEVEELEDFTLQMAHHISEKAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDS
EDYQEGMNAFLEKRKPNFVGH |
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| References |
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| External Links: | |
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| General Reference: | - Benning, M. M., Haller, T., Gerlt, J. A., Holden, H. M. (2000). "New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli." Biochemistry 39:4630-4639. Pubmed: 10769118
- 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
- Haller, T., Buckel, T., Retey, J., Gerlt, J. A. (2000). "Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli." Biochemistry 39:4622-4629. Pubmed: 10769117
- 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
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