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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR971 IGR974 IGR973 IGR975 IGR977 IGR976 IGR972 IGR970 ispF, - HD1328 ispD, - HD1329 yebM,znuC, - HD1338 lapB, - HD1332 sucB, - HD1334 sucA, - HD1336 HD1339 pckA,ppc, - HD1331 ispF, - HD1328 ispD, - HD1329 yebM,znuC, - HD1338 lapB, - HD1332 sucB, - HD1334 sucA, - HD1336 HD1339 pckA,ppc, - HD1331 ispF, - HD1328 ispD, - HD1329 yebM,znuC, - HD1338 lapB, - HD1332 sucB, - HD1334 sucA, - HD1336 HD1330 HD1330 HD1339 pckA,ppc, - HD1331
* Calculated from Protein Sequence

Gene ID: HD1334

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
sucB  

Definition:
dihydrolipoamide succinyltransferase component

Gene Start:
1092098

Gene Stop:
1090887

Gene Length:
1212

Molecular Weight*:
44730

pI*:
5.40

Net Charge*:
-8.08

EC:
2.3.1.61  

Functional Class:
Energy metabolism; TCA cycle  

Pathway: pathway table
Citrate cycle (TCA cycle)
Lysine degradation

Secondary Evidence:
Spencer,M.E., Darlison,M.G., Stephens,P.E., Duckenfield,I.K. and Guest,J.R.
Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase.
Eur. J. Biochem. 141(2): 361-374, 1984.
Medline: 84236169.

Zygmunt MS, Diaz MA, Teixeira-Gomes AP, Cloeckaert A.
Cloning, nucleotide sequence, and expression of the Brucella melitensis sucB gene coding for an immunogenic dihydrolipoamide succinyltransferase homologous protein.
Infect Immun. 2001 Oct;69(10):6537-40.
PMID: 11553602

Nguyen SV, To H, Yamaguchi T, Fukushi H, Hirai K.
Characterization of the Coxiella burnetti sucB gene encoding an immunogenic dihydrolipoamide succinyltransferase.
Microbiol Immunol. 1999;43(8):743-9.
PMID: 10524791

Spencer ME, Guest JR.
Transcription analysis of the sucAB, aceEF and lpd genes of Escherichia coli.
Mol Gen Genet. 1985;200(1):145-54.
PMID: 3897791



Comment:
0

Blast Summary:  PSI-Blast Search
Numerous significant hits using gapped BLAST to dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex from H. influenzae (1171887), E. coli (129043), Pseudomonas putida (3219722), among others.

Positions 1 to 403 are 86.6% (E value 1e-175) similar to sp|P45302|ODO2_HAEIN dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex between positions 1 and 409 in Haemophilus influenzae Rd. Positions 2 to 403 are 81.8% (E value 1e-156) similar to sp|P07016|ODO2_ECOLI dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex between positions 3 and 405 in Escherichia coli.

HD1334 is similar to dihydrolipoamide succinyltransferase from C. pneumoniae (CPn0377), C. trachomatis (CT055), (CPn0527), (CT400), (CPn0306 ), and (CT247), M. pneumoniae (MP0447), and M. genitalium (MG272). No similarities to U. urealyticum or T. pallidum.

COGS Summary:  COGS Search
BeTs to 8 clades of COG0508
COG name: Dihydrolipoamide acyltransferases
Functional Class:  C
The phylogenetic pattern of COG0508 is ----Y--cEBRH--gp--INX
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** IPB001078 (2-Oxo acid dehydrogenase acyltransferase catalytic domain) with a combined E-value of 6.1e-98.
    IPB001078A    22-54
    IPB001078B    113-143
    IPB001078C    229-250
    IPB001078D    304-346
    IPB001078E    365-401
***** IPB000089 (Biotin / Lipoyl attachment) with a combined E-value of 1.2e-24.
    IPB000089A    266-285
    IPB000089B    320-339
***** IPB003016 (2-oxo acid dehydrogenases acyltransferase component lipoyl binding site) with a combined E-value of 3.9e-14.
    IPB003016    25-59


ProDom Summary:  Protein Domain Search
Residues 18-76 are 72% similar to a (BIOTIN DIHYDROLIPOAMIDE LIPOYL CARBOXYLASE TRANSFERASE) protein domain (PD000268) which is seen in ODO2_HAEIN.

Residues 111-182 are 58% similar to a (DIHYDROLIPOAMIDE TRANSFERASE PROTEOME) protein domain (PD257045) which is seen in ODO2_HAEIN.

Residues 183-402 are 90% similar to a (DIHYDROLIPOAMIDE TRANSFERASE LIPOYL DEHYDROGENASE E2) protein domain (PD001115) which is seen in ODO2_HAEIN.



Paralogs:  Local Blast Search

HD1334 is paralogously related to HD1624 (2e-47).


Pfam Summary:  Pfam Search
Residues 3 to 76 (E-value = 1.2e-19) place HD1334 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)
Residues 111 to 147 (E-value = 2.2e-14) place HD1334 in the E3_binding family which is described as e3 binding domain (PF02817)
Residues 171 to 401 (E-value = 2.6e-143) place HD1334 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198)

PDB Hit:
pdb|1E2O| Catalytic Domain From Dihydrolipoamide Succinyltra... 411 6e-116
pdb|1B5S|A Chain A, Dihydrolipoyl Transacetylase (E.C.2.3.1.12)... 171 1e-043
pdb|1DPC| Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catal... 121 2e-028

Gene Protein Sequence:
MSIEILTPVLPESVADATVATWHKNIGETVKRDEVLVEIETDKVVLEVPA
PNDGLLTEIIQPTGSSVVPKQLLGKLSTIQAGDMAQITAKQPPQRQTTEP
RTDTHNDIDSQGPSIRRLLAEHNIEAHAIQGSGVDGRITREDIQQFLATQ
SSQQVASTDLTDSLNTIAYEDRSEKRVPMTRLRKRIAERLLEAKNSTAML
TTFNEVNMQPIMQLRKQYGEKFEKQHGVRLGFMSFYIKAVVEALKRYPEI
NASIDGEDVIYHNYFDISIAVSTPRGLVTPVIRDCDKLSMAEIEKAIKLF
ADKGRDGKLTVEELTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIK
DRPIAMNGEVVIRPMMYLALSYDHRLIDGKESVGFLVSIRDLLEDPTRLL
LEI$

Gene Nucleotide Sequence:  Sequence Viewer
ATGAGTATCGAAATTCTCACCCCCGTCCTGCCTGAGTCAGTCGCTGATGC
AACGGTTGCAACTTGGCATAAAAACATCGGCGAAACCGTCAAACGTGATG
AAGTATTAGTGGAAATTGAAACCGATAAGGTGGTGTTAGAAGTGCCCGCG
CCTAATGACGGCTTATTAACTGAAATTATCCAACCAACCGGCTCAAGTGT
TGTGCCCAAACAACTTTTAGGCAAACTTTCAACGATCCAAGCGGGCGATA
TGGCTCAAATTACTGCAAAACAACCGCCACAACGCCAAACGACTGAGCCA
CGTACAGATACACATAATGATATCGACTCACAAGGCCCATCTATACGCCG
ACTATTAGCTGAGCATAATATTGAAGCACATGCCATTCAAGGTTCAGGCG
TAGATGGCAGAATTACACGTGAAGATATCCAACAATTCCTAGCAACACAA
TCTAGCCAGCAAGTGGCGTCCACGGATTTAACGGATAGTCTAAACACGAT
TGCTTACGAAGATCGTAGCGAAAAACGCGTGCCAATGACACGCTTACGGA
AACGAATTGCAGAACGTTTACTCGAGGCTAAAAACAGCACAGCTATGCTG
ACAACCTTCAACGAAGTCAATATGCAACCGATTATGCAATTACGTAAACA
GTATGGCGAAAAATTTGAAAAACAACACGGCGTCCGCTTAGGTTTTATGT
CTTTCTATATTAAAGCGGTAGTTGAAGCCTTAAAACGTTATCCTGAAATC
AACGCATCAATTGACGGCGAAGACGTGATTTACCACAACTATTTTGATAT
TAGCATTGCGGTTTCTACACCACGAGGTTTAGTAACCCCCGTTATTCGTG
ACTGCGACAAGCTATCTATGGCAGAAATTGAAAAAGCCATCAAACTATTT
GCCGATAAAGGGCGCGATGGTAAATTAACCGTAGAAGAGCTAACTGGTGG
CAACTTCACCATTACCAACGGCGGTGTATTTGGTTCACTCATGTCAACAC
CGATTATCAATCCACCACAAAGTGCGATTTTAGGTATGCATGCTATTAAA
GATCGCCCTATTGCGATGAACGGCGAGGTCGTTATCCGCCCAATGATGTA
TTTAGCATTATCTTATGATCATCGCTTAATTGATGGTAAAGAGTCTGTCG
GCTTTTTAGTGAGCATCCGTGATTTATTAGAAGATCCAACAAGATTACTG
CTTGAGATCTGA


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