L-lactate dehydrogenase [cytochrome] (P33232)

Identification
Name:L-lactate dehydrogenase [cytochrome]
Synonyms:Not Available
Gene Name:lldD
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+)
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+2.0Ferricytochrome c+1.0Thumb ↔ 1.0Thumb+2.0Ferrocytochrome c+2.0Thumb+1.0Thumb
1.0L-Lactic acid + 2.0Ferricytochrome c + 1.0Ferricytochrome c ↔ 1.0Pyruvic acid + 2.0Ferrocytochrome c + 2.0Hydrogen ion + 1.0Ferrocytochrome c
ReactionCard
SMPDB Reactions:
1.0L-Lactic acid+1.0oxidized electron acceptor+1.0Thumb → 1.0Reduced acceptor+1.0Thumb
1.0L-Lactic acid + 1.0oxidized electron acceptor + 1.0L-Lactic acid → 1.0Reduced acceptor + 1.0Pyruvic acid
ReactionCard
1.0Thumb+1.0oxidized electron acceptor → 1.0Thumb+1.0reduced electron acceptor
1.0L-Lactic acid + 1.0oxidized electron acceptor → 1.0Pyruvic acid + 1.0reduced electron acceptor
ReactionCard
EcoCyc Reactions:
1.0an oxidized electron acceptor+1.0Thumb → 1.0a reduced electron acceptor+1.0Thumb
1.0an oxidized electron acceptor + 1.0L-Lactic acid → 1.0a reduced electron acceptor + 1.0Pyruvic acid
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Lactic acid + 1.0Ubiquinone-8 → 1.0Pyruvic acid + 1.0Ubiquinol-8
ReactionCard
1.0Thumb+1.0Menaquinone 8 → 1.0Thumb+1.0Thumb
1.0L-Lactic acid + 1.0Menaquinone 8 → 1.0Menaquinol 8 + 1.0Pyruvic acid
ReactionCard
1.0Thumb+2.0Thumb → 1.0Thumb+2.0Thumb+2.0Thumb
1.0L-Lactic acid + 2.0Ferricytochrome c → 1.0Pyruvic acid + 2.0Ferrocytochrome c + 2.0Hydrogen ion
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21652Ferricytochrome cMetaboCard
ECMDB23135Ferrocytochrome cMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00190L-Lactic acidMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
GO Classification:
Function
binding
catalytic activity
FMN binding
L-lactate dehydrogenase (cytochrome) activity
lactate dehydrogenase activity
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
Process
carboxylic acid metabolic process
cellular metabolic process
lactate metabolic process
metabolic process
monocarboxylic acid metabolic process
organic acid metabolic process
oxidation reduction
oxoacid metabolic process
Gene Properties
Blattner:b3605
Gene OrientationClockwise
Centisome Percentage:81.42
Left Sequence End3777850
Right Sequence End3779040
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:42728
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>L-lactate dehydrogenase [cytochrome]
MIISAASDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSL
ETTLFNEKLSMPVALAPVGLCGMYARRGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAI
KRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGMSGPNAAMR
RYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWI
RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGD
IAILADSGIRNGLDVVRMIALGADTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMT
LTGAKSISEITQDSLVQGLGKELPAALAPMAKGNAA
References
External Links:
ResourceLink
Uniprot ID:P33232
Uniprot Name:LLDD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742501
Ecogene ID:EG11963
Ecocyc:EG11963
ColiBase:b3605
Kegg Gene:b3605
EchoBASE ID:EB1906
CCDB:LLDD_ECOLI
BacMap:16131476
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
  • Dong, J. M., Taylor, J. S., Latour, D. J., Iuchi, S., Lin, E. C. (1993). "Three overlapping lct genes involved in L-lactate utilization by Escherichia coli." J Bacteriol 175:6671-6678. Pubmed: 8407843
  • 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
  • Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620