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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR487 IGR491 IGR488 IGR492 IGR489 CT593.1 sdhC, - CT593 sdhB, - CT591 CT594 sdhA, - CT592 dsbD,dipZ, - CT595 CT590 tolQ,exbB, - CT596 CT589 CT593.1 sdhC, - CT593 sdhB, - CT591 CT594 sdhA, - CT592 dsbD,dipZ, - CT595 CT590 tolQ,exbB, - CT596 CT589 sdhC, - CT593 sdhB, - CT591 CT594 sdhA, - CT592 dsbD,dipZ, - CT595 CT590 CT593.1 tolQ,exbB, - CT596 CT589
* Calculated from Protein Sequence

Gene ID: CT592

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
sdhA  

Definition:
fumarate reductase/succinate dehydrogenase flavoprotein subunit

Gene Start:
672768

Gene Stop:
671050

Gene Length:
1719

Molecular Weight*:
63862

pI*:
7.45

Net Charge*:
3.91

EC:
1.3.99.1  

Functional Class:
central intermediary metabolism; TCA cycle  

Pathway: pathway table
Benzoate degradation via CoA ligation
Butanoate metabolism
Carbohydrate Metabolism; Citrate cycle (TCA cycle)
Citrate cycle (TCA cycle)
Energy Metabolism; Oxidative phosphorylation
Oxidative phosphorylation
Reductive carboxylate cycle (CO2 fixation)

Comment:
Succinate dehydrogenase in B.subtilis is a trimer consisting of a flavoprotein, an iron-sulfur protein, and a cytochrome B-558. CT591 is the iron-sulfur subunit. CT593 is the cytochrome subunit. The enzyme converts succinate to fumarate in a reduction reaction.

From Prosite PDOC00393:

In bacteria two distinct, membrane-bound, enzyme complexes are responsible for the interconversion of fumarate and succinate (EC 1.3.99.1): fumarate reductase (Frd) is used in anaerobic growth, and succinate dehydrogenase (Sdh) is used in aerobic growth. Both complexes consist of two main components: a membrane-extrinsic component composed of a FAD-binding flavoprotein and an iron-sulfur protein; and an hydrophobic component composed of a membrane anchor protein and/or a cytochrome B.

In eukaryotes mitochondrial succinate dehydrogenase (ubiquinone) (EC 1.3.5.1) is an enzyme composed of two subunits: a FAD flavoprotein and and iron-sulfur protein.

The flavoprotein subunit is a protein of about 60 to 70 Kd to which FAD is covalently bound to a histidine residue which is located in the N-terminal section of the protein.


Blast Summary:  PSI-Blast Search
Hits in gapped blast to succinate dehydrogenase flavoprotein subunit
sequences, e.g. Residues 26-570 are 51% similar to
Paenibacillus macerans(Y08563). No similarities to T.pallidum or M.genitalium.

CT592 is orthologously related to CPn0789 and
they share 80% similarity.

COGS Summary:  COGS Search
BeTs to 12 clades of COG1053
COG name: Succinate dehydrogenase/fumarate reductase, flavoprotein subunits
Functional Class: C
The phylogenetic pattern of COG1053 is Amt-YqvcEbRhuj----inx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 7-21, 32-50, 54-83, 92-120, 125-142, 215-265, 353-379, 399-430, 502-555
are matched to blocks BL00504A,B,C,D,E,F,G,H,I, concerned with ,
Fumarate reductase / succinate dehydrogenase FAD-binding site proteins, e.g. DHSA_BACSU.
Residues 7-26 are matched to block PR00757A, concerned with
FLAVIN-CONTAINING AMINE OXIDASE SIGNATURE, e.g. AOFA_BOVIN.
Residues 7-29, 5-20 are matched to blocks PR00420A,B, concerned with
AROMATIC-RING HYDROXYLASE (FLAVOPROTEIN MONOOXYGENASE) SIGNATURE, e.g. TCMG_STRGA.
Residues 7-29, 8-22 are matched to blocks PR00419A,D, concerned with
ADRENODOXIN REDUCTASE FAMILY SIGNATURE, e.g. GLSN_MEDSA.
Residues 7-22, 6-24 are matched to blocks PR00370A,D, concerned with
FLAVIN-CONTAINING MONOOXYGENASE (FMO) SIGNATURE, e.g. HSFMO5.
Residues 7-24 are matched to blocks BL00677A, concerned with
D-amino acid oxidases proteins, e.g. OXDA_RHOGC.
Residues 9-40 are matched to blocks BL00982A, concerned with
Bacterial-type phytoene dehydrogenase proteins, e.g. CRTI_MYXXA.
Residues 10-31, 167-204 are matched to blocks BL00573A,F, concerned with
Pyridine nucleotide-disulphide oxidoreductases class-II, e.g. DHNA_BACSU.
Residues 7-21 are matched to block PR00335A, concerned with TRKA POTASSIUM
UPTAKE PROTEIN SIGNATURE, e.g. KEFC_ECOLI.
Residues 7-48, 225-257 are matched to blocks BL01280A,E, concerned with
Glucose inhibited division protein A family proteins, e.g. GIDA_ECOLI.

ProDom Summary:  Protein Domain Search
Residues 26-205 are 57% similar to a SUCCINATE DEHYDROGENASE
FLAVOPROTEIN SUBUNIT domain as observed in DHSA_BACSU.
Residues 208-260, 276-436, 449-554 support this assignment.
Residues 47-200 are 31% similar to a domain from FRDA_SHEPU,
concerned with fumarate reductase flavoprotein subunit precursor
domain.
Also residues 482-565 are 29% similar to a domain from Y033_METJA,
that is a hypothetical FAD flavoprotein oxidase.

Paralogs:  Local Blast Search
No evidence of paralogs in C. trachomatis.

Pfam Summary:  Pfam Search
Residues 107 to 462 (E-value = 1.1e-87) place CT592 in the FAD_binding_2 family which is described as FAD binding domain (PF00890)
Residues 480 to 572 (E-value = 1e-23) place CT592 in the Succ_DH_flav_C family which is described as Fumarate reductase/succinate dehydrogenase flavoprotein C-terminal domain (PF02910)

Structural Feature(s):
Feature Type  Start  Stop
coil-coil  
490  
520

PDB Hit:
none

Gene Protein Sequence:
MMNQRCRVIIIGGGLAGLSAAMQLADRGILVELFSLTKVKRSHSVCAQGG
INAALNLKGENDSPYIHAYDTIKGGDFLADQPPVLEMCLTAPRIIHMLDR
FGCPFNRDADGNLDVRRFGGTLYHRTVFCGASTGQQLMYTMDEQVRRREC
QGKIIKRENHEFVRLITNTEGRACGVVVMNLFNHRLEVIQGDAVIIATGG
LGVIFKMSTNSTICTGAANGRLFMQGMHYANPEFIQIHPTAISGLDKLRL
ISESVRGEGGRVWVPGCSSKTIIFPDGSRRPCGETGKPWYFLEEMYPAYG
NLVSRDVGARAILQVCEAGLGIDGRHEVFLDVTHLPVETLNKLEAVLDIY
HKFTGEDPKKVPMRIFPAVHYSMGGAWVDWPASDDRDRDSRYRHMTNIPG
CFNCGESDFQYHGANRLGANSLLACLYAGLVAGDEAARFVESFGSCIYSQ
QDLNQALQQELEISREILSRQGGENAFALHEEIARVMVSNVTVKRENKAL
EETLHKLKEFRERIKKVSVHDSSRFANKTFHFVRQMEPMLELALAITTGA
LLRNEFRGSHYKPEFSKRDDVNG

Gene Nucleotide Sequence:  Sequence Viewer
ATGATGAATCAGCGTTGTCGAGTCATTATCATTGGAGGAGGACTTGCTGG
GCTATCTGCCGCTATGCAACTCGCAGATCGTGGTATTTTAGTAGAGCTGT
TCTCTTTAACTAAGGTCAAGCGATCGCATTCTGTATGTGCACAGGGAGGA
ATTAATGCAGCCTTGAATCTCAAAGGAGAAAATGATTCCCCATACATTCA
TGCTTACGATACGATAAAAGGAGGGGATTTTTTAGCAGATCAGCCTCCTG
TATTGGAAATGTGTTTAACCGCTCCACGCATTATTCATATGCTGGATAGG
TTCGGGTGTCCATTTAACCGTGATGCAGATGGAAACCTCGATGTGCGGCG
TTTCGGAGGGACTCTCTATCATCGCACAGTCTTTTGTGGAGCGTCCACAG
GGCAGCAGTTAATGTACACCATGGATGAGCAGGTACGTCGTCGTGAATGT
CAAGGGAAGATCATTAAAAGAGAAAATCATGAATTTGTTCGATTGATTAC
CAATACGGAAGGAAGAGCTTGTGGCGTTGTCGTCATGAATTTATTCAATC
ACCGTTTAGAGGTTATACAAGGTGATGCGGTGATTATTGCAACGGGTGGT
TTGGGTGTCATTTTTAAAATGTCTACCAACTCGACTATCTGTACAGGAGC
TGCAAATGGTCGATTATTCATGCAAGGCATGCACTATGCGAATCCTGAAT
TTATTCAAATTCATCCGACAGCAATTTCTGGACTAGATAAGTTGCGTTTG
ATTTCTGAATCGGTTCGTGGTGAAGGAGGAAGAGTTTGGGTGCCTGGGTG
TTCATCCAAAACGATTATTTTCCCTGATGGTTCGCGACGCCCTTGCGGAG
AGACAGGCAAGCCTTGGTATTTTCTAGAAGAGATGTATCCTGCTTACGGC
AATTTAGTGAGTCGAGATGTCGGAGCGCGAGCTATTTTACAGGTATGTGA
GGCAGGTCTGGGTATTGATGGTCGTCACGAAGTGTTTTTAGATGTAACCC
ATCTACCTGTAGAGACTCTGAATAAGCTAGAGGCTGTTTTAGATATCTAT
CATAAATTTACAGGTGAAGATCCTAAAAAAGTCCCTATGCGCATTTTTCC
TGCGGTGCACTATTCTATGGGAGGCGCCTGGGTAGATTGGCCTGCCAGTG
ACGATAGGGATCGCGATAGTCGCTATCGACATATGACGAATATCCCAGGT
TGTTTTAATTGTGGCGAGTCAGATTTTCAATATCATGGAGCCAATCGTTT
AGGAGCTAATTCTTTGTTAGCGTGTTTATACGCTGGGTTAGTCGCAGGAG
ATGAAGCGGCACGATTTGTGGAATCGTTCGGAAGTTGTATCTATTCCCAA
CAAGATCTTAATCAAGCTTTGCAACAAGAGCTAGAGATCTCTCGAGAGAT
TCTCTCTCGTCAAGGAGGAGAAAATGCATTTGCTTTGCATGAAGAGATCG
CGCGAGTCATGGTCAGTAATGTGACCGTGAAAAGGGAGAACAAGGCTCTT
GAAGAAACTCTACACAAGTTAAAGGAGTTTAGAGAAAGAATAAAAAAAGT
TTCGGTACACGATTCTTCTCGATTTGCGAATAAAACGTTTCATTTTGTTC
GACAAATGGAACCTATGTTAGAGCTTGCACTAGCTATCACGACAGGAGCT
TTATTAAGAAACGAATTTCGAGGGTCTCATTACAAACCAGAATTTTCGAA
ACGAGATGATGTGAATGGT


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