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Treponema pallidum Search Results

Record: 1 of 1  
MiniMap IGR27 IGR24 IGR32 IGR30 IGR29 IGR25 IGR28 IGR26 IGR31 TP0033 TP0032 TP0034 ldh, - TP0037 TP0038 TP0041 TP0039 TP0031 TP0035 TP0036 TP0042 mcp-1, - TP0040 TP0033 TP0032 TP0034 ldh, - TP0037 TP0038 TP0041 TP0039 TP0031 TP0035 TP0036 TP0042 mcp-1, - TP0040 Type: tandem, Name:  - 14 Type: tandem, Name:  - 11 Type: tandem, Name:  - 12 Type: tandem, Name:  - 13 TP0033 TP0032 TP0034 ldh, - TP0037 TP0038 TP0039 TP0031 TP0035 TP0036 TP0042 mcp-1, - TP0040 TP0041
* Calculated from Protein Sequence

Gene ID: TP0037

DNA Molecule Name:
1  

Genbank ID:
3322294

Gene Name:
ldh  

Definition:
D-lactate dehydrogenase

Gene Start:
45557

Gene Stop:
44565

Gene Length:
993

Molecular Weight*:
36860

pI*:
6.71

Net Charge*:
-1.29

EC:
1.1.1.28  

Functional Class:
Energy metabolism; Fermentation  

Pathway: pathway table
Carbohydrate metabolism; Pyruvate metabolism

Comment:
First component of the membrane bound D-lactate oxidase.
Catalytic activity: D-LACTATE + NAD(+) = PYRUVATE + NADH

There is a 3D structure of L-Lactate Dehydrogenase of Bifidobacterium.

Blast Summary:  PSI-Blast Search
Significant hits to many D-Lactate Dehydrogenases:
for example residues 2- 331 are 35% similar to M85224, D-lactate
dehydrogenase [Lactobacillus delbrueckii]. Additionally there were
significant hits to many other dehydrogenases:
for example residues 1- 329 are 29% similar to U32694,
2-hydroxyacid dehydrogenase homolog (ddh) [Haemophilus influenzae]

COGS Summary:  COGS Search
BeTs to 5 clades of COG1052
COG name: Lactate dehydrogenase and related dehydrogenases
Functional Class:  C,H,R
The phylogenetic pattern of COG1052 is a--KYq-CEBrHuj---l---
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
Residues 148- 158, 210- 264, 32- 86, 77- 131 and 294- 304 represent a
significant (100%) match to blocks (BL00065)D-isomer specific 2-
hydroxyacid dehydrogenases NAD-binding site.
Residues 148-184 also represent a significant (95%+) but low complexity
hit to blocks (BL00071)Glyceraldehyde 3-phosphate dehydrogenase proteins,
blocks (PR00335) TRKA POTASSIUM UPTAKE PROTEIN SIGNATURE, blocks
(BL00836) Alanine dehydrogenase & pyridine nucleotide transhydrogenase
and blocks (PR00419) ADRENODOXIN REDUCTASE FAMILY SIGNATURE. Residues
196- 242 also has significant but low complexity match to blocks
(BL00836) Alanine dehydrogenase & pyridine nucleotide transhydrogenase.

ProDom Summary:  Protein Domain Search
Residues 130- 271 are 51% similar to DEHYDROGENASE FORMATE domain of
LDHD_LACPL. Residues 79-115 are 54% similar to the DEHYDROGENASE
FORMATE domain of DHD2_LACCA. Residues 277- 308 are 50% similar to
D-LACTATE DEHYDROGENASE domain of LDHD_LACPL. Residues 6-45 are 51%
similar to DEHYDROGENASE D-LDH domain of LDHD_LEUME (the E value is
low).

Paralogs:  Local Blast Search
There is no evidence of paralogs in T. pallidum.

Pfam Summary:  Pfam Search
Residues 3 to 100 (E-value = 2.9e-21) place TP0037 in the 2-Hacid_dh family which is described as D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain (PF00389)
Residues 106 to 296 (E-value = 1.7e-68) place TP0037 in the 2-Hacid_dh_C family which is described as D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826)

PDB Hit:
gi|2392297|pdb|1DXY| Structure Of D-2-Hydroxyisocaproate Dehydrogenase D-2-Hydroxycarboxylate Dehydrogenase, D-Lactate Dehydrogenase, Oxidoreductase Mol_id: 1; Molecule: D-2-Hydroxyisocaproate Dehydrogenase; Chain: Null; Synonym: D-Hicdh, R-Hicdh, R-2...

Gene Protein Sequence:
MRCVVFNLREEEAPYVEKWKQSHPGVVVDTYEEPLTAKNKELLKGYEGLV
VMQFLAMEDEVYDYMGACKLKVLSTRTAGFDMYNATLLKKHGIRLTNVPS
YSPNAIGEYALAAALQLTRHAREIETFVRKRDFRWQKPILSKELRCSRVG
ILGTGRIGQAAARLFKGVGAQVVGFDPYPNDAAKEWLTYVSMDELLSTSD
VISLHMPATKDSHHLINAKTIAQMKDGVYLVNTARGAVIDSQALLDSLDK
GKIAGAALDAYEFEGPYIPKDNGNNPITDTVYARLVAHERIIYTPHIAFY
TETAIENMVFNSLDACTTVLRGEPCAAEIKL

Gene Nucleotide Sequence:  Sequence Viewer
ATGAGGTGTGTTGTCTTTAATCTTCGAGAAGAAGAAGCCCCTTACGTGGA
GAAGTGGAAGCAGTCCCATCCAGGGGTAGTCGTGGACACTTACGAGGAAC
CGTTGACCGCAAAGAACAAGGAGTTGCTTAAGGGGTATGAAGGGCTCGTG
GTTATGCAGTTTCTCGCTATGGAAGACGAGGTGTATGACTACATGGGTGC
GTGCAAACTAAAAGTCCTTTCCACACGTACCGCAGGCTTTGATATGTATA
ATGCAACTTTGCTGAAAAAGCACGGCATCCGGCTGACGAACGTACCGTCC
TATTCACCGAATGCTATCGGGGAATATGCACTCGCCGCCGCGTTGCAGCT
GACGCGACATGCGCGCGAGATTGAAACTTTTGTAAGGAAGCGTGATTTTC
GCTGGCAAAAACCAATTCTCTCGAAGGAGCTCCGCTGCTCACGCGTAGGT
ATCTTGGGAACGGGCAGGATTGGACAGGCAGCAGCAAGGCTCTTCAAAGG
GGTTGGTGCTCAGGTAGTTGGTTTTGATCCGTACCCGAACGATGCCGCAA
AGGAATGGTTAACCTACGTGAGTATGGACGAGCTGCTGTCCACTAGCGAC
GTGATCAGCTTGCACATGCCTGCGACAAAGGACAGTCATCACCTGATCAA
TGCGAAAACAATCGCGCAGATGAAAGATGGCGTGTACCTGGTGAACACGG
CACGCGGAGCAGTGATCGACAGTCAGGCGCTCTTAGACAGCTTGGACAAA
GGCAAGATTGCAGGTGCTGCACTGGATGCGTACGAGTTTGAGGGTCCGTA
TATTCCTAAAGACAACGGGAACAACCCTATTACCGATACGGTCTATGCTC
GGCTTGTCGCACATGAGCGTATCATCTATACCCCTCATATCGCCTTCTAC
ACAGAAACAGCGATAGAGAACATGGTATTCAATTCGCTTGACGCCTGCAC
CACGGTGCTGCGTGGGGAGCCTTGTGCCGCTGAAATCAAGCTG


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