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Treponema pallidum Search Results

Record: 1 of 1  
MiniMap IGR61 IGR62 IGR59 IGR60 IGR63 IGR64 TP0082 TP0080 malG, - TP0076 TP0081 malF, - TP0075 cap, - TP0077 xdh, - TP0079 TP0082 TP0080 malG, - TP0076 TP0081 malF, - TP0075 cap, - TP0077 xdh, - TP0079 Type: tandem, Name:  - 22 TP0082 TP0080 malG, - TP0076 TP0081 malF, - TP0075 cap, - TP0077 xdh, - TP0079 TP0078 TP0078
* Calculated from Protein Sequence

Gene ID: TP0079

DNA Molecule Name:
1  

Genbank ID:
3322338

Gene Name:
xdh  

Definition:
xanthine dehydrogenase homolog/ xanthine oxidase homolog

Gene Start:
87041

Gene Stop:
89260

Gene Length:
2220

Molecular Weight*:
81773

pI*:
7.54

Net Charge*:
7.17

EC:
1.1.1.204  1.1.3.22  

Functional Class:
Purines, pyrimidines, nucleosides, and nucleotides; Salvage of nucleosides and nucleotides  

Pathway: pathway table
Nucleotide metabolism; Purine Metabolism

Secondary Evidence:
Xi H, Schneider BL, Reitzer L.
Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage.
J Bacteriol. 2000 Oct;182(19):5332-41.
PMID: 10986234

Leimk├╝hler S, Kern M, Solomon PS, McEwan AG, Schwarz G, Mendel RR, Klipp W.
Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes.
Mol Microbiol. 1998 Feb;27(4):853-69.
PMID: 9515710

Comment:
This enzyme can act on a variety of purines and aldehydes.

In humans it can be converted from the dehyrogenase form (D) to the
oxidase form (O) irreversibly by proteolysis or reversibly through
the oxidation of sulfhydril groups.

Xanthine Dehydrogenase -> XANTHINE + NAD(+) + H(2)O = URATE + NADH.
Xanthine Oxidase -> XANTHINE + H(2)O + O(2) = URATE + H(2)O(2).

Blast Summary:  PSI-Blast Search
Gapped BLAST revealed the N-terminal and middle region had several
significant hits to xanthine dehydrogenases. For example residues
60-381 are 23% similar to xanthine dehydrogenase of Rhodobacter
capsulatus,(AJ001013).

COGS Summary:  COGS Search
BeTs to 3 clades of COG1529
COG name: Oxidoreductases related to 4-hydroxybenzoyl-CoA reductase
Functional Class:? R
The phylogenetic pattern of COG1529 is -----q--Ebr------l---
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
None.

ProDom Summary:  Protein Domain Search
Residues 25-344 are 20% similar to XANTHINE DEHYDROGENASE of XDH_CALVI.
Residues 355-369, 494-524, 601-629 and 708-721 were also very similar
to XANTHINE DEHYDROGENASE XD OXIDASE from various organisms.

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

Pfam Summary:  Pfam Search
Residues 26 to 125 (E-value = 6.2e-27) place TP0079 in the Ald_Xan_dh_C family which is described as Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain (PF01315)
Residues 129 to 674 (E-value = 4e-157) place TP0079 in the Ald_Xan_dh_C2 family which is described as Aldehyde oxidase and xanthine dehydrogenase, molybdopterin binding domain (PF02738)

PDB Hit:
none

Gene Protein Sequence:
MRGVCDRDRGAHRTRMCKGKSIYMSVFVSDGARTGSVYAQLVRAPRVAGL
LLNIDIPSLPDGYSFYTAAHIPGCNAVRCGENTVPVFAHGEVVYAGEPVG
ILIGPDEHVVRNLVQDVVVHTCAERACASEILCGISEGEPLAQKVAVQGD
AETAFKRASHTVCSSCTFEPRVHYFAEMPEVQALPDAHGLHVYAATQWPA
HMRKTIAQVLNISEHAVHVHPQQEALSCDGRIWFPSVMASQAALAAYCAK
KPVRLSFSFQEYVQYCPKTPKITIAHRTALNAAHAVEGMFVFISLDAGAG
NLLIDRMVAHMVHTALGNYEIPRYRIECTAFRSNVGLTDVFNGWADAYTS
NALEMHINQLCAELHIFPDEWRVAHMKDTRETQRFARLLAYLCEEGDFRR
KHAAFSMVNAVRKAHDTHAWRGIGLALGFQYDPSAMLARSGFSYVLQMTL
HTDARIVVHSVPLSDSFKRVVVAFLIREFACLEDAIFFKSSDEAYGVDLL
GPSVESVGMRVFARLVRKCVRAIQRQRFRKPLPITVQGSFNTAKKGQVYQ
VVTVAKSDVSVPDAQSEQCASKVPVTADTSGKCEDMNGFTKMHGMSTHTP
AACIIELELDALCVQPKIVRLWFVCDPGYVFCEKDVYRTVSRSITRALSH
VSVEKIWERARTPEYVIIDPSDTPPYHVTLLSSNAAARAVGTVAEGIVPA
AYYAALRQILPISQNATHKVPFVARDIFYEMFSLSADDSL

Gene Nucleotide Sequence:  Sequence Viewer
TTGCGTGGCGTATGTGATAGAGACCGTGGTGCGCACCGCACAAGAATGTG
CAAAGGGAAGAGCATATATATGAGCGTGTTCGTTTCAGACGGTGCGCGCA
CAGGGAGCGTCTATGCACAGCTTGTCCGTGCGCCGCGCGTTGCAGGATTG
CTGCTGAACATAGATATTCCCTCTCTCCCTGACGGGTACTCTTTTTATAC
TGCAGCACATATTCCCGGATGCAATGCCGTTCGGTGTGGGGAAAATACTG
TGCCGGTTTTTGCGCATGGAGAGGTGGTGTACGCAGGGGAACCGGTGGGT
ATCCTCATTGGGCCTGATGAGCATGTGGTACGTAATTTAGTGCAAGATGT
GGTGGTGCATACGTGCGCAGAGCGGGCCTGTGCGTCGGAAATACTCTGTG
GAATCAGTGAAGGGGAACCCCTCGCTCAAAAGGTGGCGGTGCAAGGAGAT
GCAGAAACTGCTTTTAAACGCGCATCACACACGGTATGCTCCTCTTGTAC
ATTTGAGCCGCGTGTACACTACTTTGCGGAAATGCCAGAAGTACAGGCAC
TACCCGACGCGCACGGTCTGCACGTGTACGCTGCTACGCAGTGGCCTGCG
CACATGAGAAAAACTATCGCGCAGGTACTGAATATTTCTGAGCATGCGGT
GCACGTACATCCGCAGCAGGAAGCGCTTTCCTGTGATGGGAGAATATGGT
TCCCCTCAGTGATGGCAAGTCAGGCGGCGCTTGCAGCCTATTGTGCGAAA
AAGCCGGTACGCTTGTCTTTTTCCTTTCAAGAGTATGTGCAGTACTGTCC
TAAGACTCCCAAGATTACCATTGCACATCGCACGGCGCTCAACGCCGCGC
ATGCGGTAGAAGGTATGTTTGTTTTTATCTCCCTCGATGCAGGAGCGGGG
AATTTATTGATCGATCGTATGGTTGCGCATATGGTCCATACTGCATTAGG
AAATTATGAAATTCCTCGGTACCGCATTGAATGCACAGCGTTTCGTTCAA
ATGTTGGATTAACGGATGTTTTTAATGGATGGGCAGATGCATACACTTCT
AATGCATTAGAAATGCATATTAATCAGTTATGTGCTGAGCTTCATATATT
CCCTGACGAGTGGCGTGTGGCGCACATGAAAGATACGCGGGAAACACAGC
GTTTTGCGCGGTTGCTCGCCTATCTGTGTGAGGAAGGAGATTTTCGTCGA
AAGCACGCAGCCTTCAGCATGGTCAATGCAGTACGAAAAGCACATGACAC
CCATGCCTGGCGTGGTATTGGACTCGCGTTGGGGTTTCAATATGATCCGT
CTGCGATGTTAGCCCGTTCGGGTTTTTCCTATGTATTACAAATGACGCTG
CACACTGATGCGCGCATTGTGGTGCACAGCGTTCCGCTTTCTGATTCGTT
TAAACGGGTAGTGGTTGCGTTTCTCATCAGAGAGTTTGCGTGTCTGGAGG
ATGCGATCTTTTTTAAAAGTAGTGATGAGGCGTATGGCGTGGATCTGTTG
GGTCCGTCTGTGGAATCAGTGGGGATGAGGGTGTTTGCACGGTTGGTGAG
AAAGTGTGTACGAGCAATTCAGAGACAACGCTTCAGAAAGCCACTTCCTA
TCACGGTACAGGGGTCCTTTAACACGGCCAAGAAGGGGCAGGTGTATCAA
GTGGTGACTGTTGCTAAGTCAGATGTTTCGGTGCCCGATGCGCAATCTGA
GCAGTGTGCCTCAAAGGTACCTGTGACTGCTGATACTAGCGGAAAATGTG
AGGATATGAACGGTTTTACCAAAATGCACGGAATGAGCACGCACACTCCT
GCAGCCTGTATTATTGAACTCGAATTAGATGCGTTGTGCGTGCAACCTAA
GATTGTCAGGTTGTGGTTTGTTTGCGATCCTGGGTATGTCTTTTGTGAAA
AAGATGTGTACCGTACCGTGAGTCGAAGCATTACTCGTGCGCTTTCGCAC
GTATCTGTAGAAAAGATTTGGGAGCGTGCGCGCACACCCGAGTATGTTAT
CATCGATCCATCCGATACTCCTCCCTATCACGTCACCCTTTTGAGTTCAA
ATGCTGCTGCGCGTGCGGTGGGAACGGTTGCCGAAGGTATTGTTCCTGCT
GCGTACTACGCAGCACTGCGGCAAATTTTGCCGATTTCTCAAAACGCTAC
CCATAAGGTTCCTTTTGTTGCGCGGGATATTTTTTATGAGATGTTTTCCC
TCAGTGCAGACGATTCTCTA


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