Anaerobic glycerol-3-phosphate dehydrogenase subunit C (P0A996)

Identification
Name:Anaerobic glycerol-3-phosphate dehydrogenase subunit C
Synonyms:
  • G-3-P dehydrogenase
Gene Name:glpC
Enzyme Class:
Biological Properties
General Function:Involved in iron-sulfur cluster binding
Specific Function:Electron transfer protein; may also function as the membrane anchor for the glpAB dimer
Cellular Location:Cell inner membrane; Peripheral membrane protein.
SMPDB Pathways:
  • glycerol metabolism PW000914
  • glycerol metabolism II PW000915
  • glycerol metabolism III (sn-glycero-3-phosphoethanolamine) PW000916
  • glycerol metabolism IV (glycerophosphoglycerol) PW000917
  • glycerol metabolism V (glycerophosphoserine) PW000918
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Glycerol 3-phosphate + 1.0FAD ↔ 1.0Dihydroxyacetone phosphate + 1.0FADH2
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Glycerol 3-phosphate + 1.0Quinone ↔ 1.0Dihydroxyacetone phosphate + 1.0Hydroquinone
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0menaquinone-8 → 1.0Thumb+1.0Thumb
1.0Glycerol 3-phosphate + 1.0menaquinone-8 → 1.0Menaquinol 8 + 1.0Dihydroxyacetone phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Glycerol 3-phosphate + 1.0Ubiquinone-8 → 1.0Dihydroxyacetone phosphate + 1.0Ubiquinol-8
ReactionCard
1.0Thumb+1.0Menaquinone 8 → 1.0Thumb+1.0Thumb
1.0Glycerol 3-phosphate + 1.0Menaquinone 8 → 1.0Dihydroxyacetone phosphate + 1.0Menaquinol 8
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Demethylmenaquinone 8 + 1.0Glycerol 3-phosphate → 1.02-Demethylmenaquinol 8 + 1.0Dihydroxyacetone phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211542-Demethylmenaquinol 8MetaboCard
ECMDB211552-Demethylmenaquinone 8MetaboCard
ECMDB01473Dihydroxyacetone phosphateMetaboCard
ECMDB01248FADMetaboCard
ECMDB01197FADH2MetaboCard
ECMDB00126Glycerol 3-phosphateMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
GO Classification:
Component
cell part
membrane
Function
binding
catalytic activity
electron carrier activity
iron-sulfur cluster binding
metal cluster binding
oxidoreductase activity
Process
establishment of localization
metabolic process
oxidation reduction
transport
Gene Properties
Blattner:b2243
Gene OrientationClockwise
Centisome Percentage:50.73
Left Sequence End2353543
Right Sequence End2354733
Gene Sequence:
>1191 bp
ATGACAACAAACACTGTTTCCCGCAAAGTGGCGTGGCTACGGGTCGTTACGCTGGCAGTC
GCCGCCTTCATCTTCAACACCACCGAATTTGTCCCTGTTGGCCTGCTCTCTGACATTGCG
CAAAGTTTTCACATGCAAACCGCTCAGGTCGGCATCATGTTGACCATTTACGCATGGGTA
GTAGCGCTAATGTCATTGCCTTTTATGTTAATGACCAGTCAGGTTGAACGGCGCAAATTA
CTGATCTGCCTGTTTGTGGTGTTTATTGCCAGCCACGTACTGTCGTTTTTGTCGTGGAGC
TTTACCGTTCTGGTGATCAGTCGCATTGGTGTGGCTTTTGCACATGCGATTTTCTGGTCG
ATTACGGCGTCTCTGGCGATCCGTATGGCTCCGGCCGGGAAGCGAGCACAGGCATTGAGT
TTAATTGCCACCGGTACAGCACTGGCGATGGTCTTAGGTTTACCTCTCGGGCGCATTGTG
GGCCAGTATTTCGGTTGGCGAATGACCTTCTTCGCGATTGGTATTGGGGCGCTTATCACC
CTTTTGTGCCTGATTAAGTTACTTCCCTTACTGCCCAGTGAGCATTCCGGTTCACTGAAA
AGCCTCCCGCTATTGTTCCGCCGCCCGGCATTGATGAGCATTTATTTGTTAACTGTGGTG
GTTGTCACCGCCCATTACACGGCATACAGCTATATCGAGCCTTTTGTACAAAACATTGCG
GGATTCAGCGCCAACTTTGCCACGGCATTACTGTTATTACTCGGTGGTGCGGGCATTATT
GGCAGCGTGATTTTCGGTAAACTGGGTAATCAGTATGCGTCTGCGTTGGTGAGTACGGCG
ATTGCGCTGTTGCTGGTGTGCCTGGCATTGCTGTTACCTGCGGCGAACAGTGAAATACAC
CTCGGGGTGCTGAGTATTTTCTGGGGGATCGCGATGATGATCATCGGGCTTGGTATGCAG
GTTAAAGTGCTGGCGCTGGCACCAGATGCTACCGACGTCGCGATGGCGCTATTCTCCGGC
ATATTTAATATTGGAATCGGGGCGGGTGCGTTGGTAGGTAATCAGGTGAGTTTGCACTGG
TCAATGTCGATGATTGGTTATGTGGGCGCGGTGCCTGCTTTTGCCGCGTTAATTTGGTCA
ATCATTATATTTCGCCGCTGGCCAGTGACACTCGAAGAACAGACGCAATAG
Protein Properties
Pfam Domain Function:
Protein Residues:396
Protein Molecular Weight:44108
Protein Theoretical pI:9
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Anaerobic glycerol-3-phosphate dehydrogenase subunit C
MNDTSFENCIKCTVCTTACPVSRVNPGYPGPKQAGPDGERLRLKDGALYDEALKYCINCK
RCEVACPSDVKIGDIIQRARAKYDTTRPSLRNFVLSHTDLMGSVSTPFAPIVNTATSLKP
VRQLLDAALKIDHRRTLPKYSFGTFRRWYRSVAAQQAQYKDQVAFFHGCFVNYNHPQLGK
DLIKVLNAMGTGVQLLSKEKCCGVPLIANGFTDKARKQAITNVESIREAVGVKGIPVIAT
SSTCTFALRDEYPEVLNVDNKGLRDHIELATRWLWRKLDEGKTLPLKPLPLKVVYHTPCH
MEKMGWTLYTLELLRNIPGLELTVLDSQCCGIAGTYGFKKENYPTSQAIGAPLFRQIEES
GADLVVTDCETCKWQIEMSTSLRCEHPITLLAQALA
References
External Links:
ResourceLink
Uniprot ID:P0A996
Uniprot Name:GLPC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742501
Ecogene ID:EG10393
Ecocyc:EG10393
ColiBase:b2243
Kegg Gene:b2243
EchoBASE ID:EB0388
CCDB:GLPC_ECOLI
BacMap:16130178
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
  • Cole, S. T., Eiglmeier, K., Ahmed, S., Honore, N., Elmes, L., Anderson, W. F., Weiner, J. H. (1988). "Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12." J Bacteriol 170:2448-2456. Pubmed: 3286606
  • 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
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837