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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR869 IGR872 IGR870 IGR868 IGR867 IGR871 IGR866 fabZ, - HD1188 skp,omp26, - HD1190 lpxA, - HD1187 firA,lpxD, - HD1189 ecfE,yaeL, - HD1192 HD1183 D15, - HD1191 dxr, - HD1186 ppG,relA, - HD1185 fabZ, - HD1188 skp,omp26, - HD1190 lpxA, - HD1187 firA,lpxD, - HD1189 ecfE,yaeL, - HD1192 HD1183 D15, - HD1191 dxr, - HD1186 ppG,relA, - HD1185 fabZ, - HD1188 skp,omp26, - HD1190 lpxA, - HD1187 firA,lpxD, - HD1189 ecfE,yaeL, - HD1192 HD1183 D15, - HD1191 dxr, - HD1186 ppG,relA, - HD1185
* Calculated from Protein Sequence

Gene ID: HD1188

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
fabZ  

Definition:
(3R)-hydroxymyristoyl-acyl carrier protein dehydrase

Gene Start:
967667

Gene Stop:
967203

Gene Length:
465

Molecular Weight*:
17345

pI*:
6.50

Net Charge*:
-0.66

EC:
4.2.1.-  

Functional Class:
Fatty acid and phospholipid metabolism  

Pathway: pathway table
Bile acid biosynthesis
Butanoate metabolism
Cyanoamino acid metabolism
Fructose and mannose metabolism
Phenylalanine metabolism
Tryptophan metabolism
Tyrosine metabolism

Secondary Evidence:
Servos,S., Khan,S. and Maskell,D.
Cloning and expression of genes encoding lipid A biosynthesis from
Haemophilus influenzae type b
Gene 175 (1-2), 137-141 (1996)
MEDLINE: 97074663

Coleman,J. and Raetz,C.R.
First committed step of lipid A biosynthesis in Escherichia coli:
sequence of the lpxA gene
J. Bacteriol. 170 (3), 1268-1274 (1988)
MEDLINE: 88139188

Mohan,S., Kelly,T.M., Eveland,S.S., Raetz,C.R. and Anderson,M.S.
An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis
J. Biol. Chem. 269 (52), 32896-32903 (1994)
MEDLINE: 95105173

Heath RJ, Rock CO.
Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis.
J Biol Chem. 1996 Nov 1;271(44):27795-801.
PMID: 8910376

Comment:
For other "fab" genes, see HD1266 (fabI), HD0612 (fabB), HD0707 (fabD), HD0708 (fabG), HD0774 (fabH).

Blast Summary:  PSI-Blast Search
Many significant hits using gapped BLAST to (3R)-hydroxymyristoyl-acyl carrier protein dehydratase from H. influenzae (1169597), Yersinia enterocolitica (418334), E. coli (544275), among others.

HD is similar to (3R)-hydroxymyristoyl-acyl carrier protein dehydratase from C. pneumoniae (CPn0651) and C. trachomatis (CT532). No similarities to U. urealyticum, T. pallidum, M. genitalium, or M. pneumoniae.

COGS Summary:  COGS Search
BeTs to 8 clades of COG0764
COG name: 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratases
Functional Class:  I
The phylogenetic pattern of COG0764 is -----qvcEB-Huj----inx
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** IPB001143 (Bacterial thioester dehydrase) with a combined E-value of 3.3e-78.
    IPB001143A    18-31
    IPB001143B    34-87
    IPB001143C    97-139


ProDom Summary:  Protein Domain Search
Residues 53-147 are 65% similar to a (LIPID DEHYDRATASE SYNTHESIS LYASE) protein domain (PD226032) which is seen in FABZ_HAEIN.

Residues 12-52 are 75% similar to a (CARRIER DEHYDRATASE LIPID COMPLETE) protein domain (PD416034) which is seen in Q9CJK9_PASMU.

Residues 53-142 are 77% similar to a (CARRIER DEHYDRATASE COMPLETE PROTEOME) protein domain (PD005671) which is seen in Q9CJK9_PASMU.



Paralogs:  Local Blast Search

HD1188 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 58 to 147 (E-value = 3.8e-20) place HD1188 in the 4HBT family which is described as Thioesterase superfamily (PF03061)

PDB Hit:
No significant hits to the NCBI PDB database.

Gene Protein Sequence:
MAIETAENRTPKVIEVTEIMNMLPHRYPFLLVDRVTDYEEGKWLRAIKNV
TVNEPCFTGHFPSSPVFPGVLILEAMAQATGVLAVATYGKMREDELYYFA
AIDNARFKRPVVPGDQLVLEVEFLKEIRGITKFTGKAYVNGKLACEADLM
CARK$

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCGATTGAAACAGCAGAAAATCGAACCCCTAAGGTTATTGAAGTTAC
TGAGATTATGAATATGCTACCACATCGTTATCCTTTTCTTTTAGTGGATC
GTGTAACAGATTATGAAGAAGGCAAATGGTTGAGAGCAATCAAAAATGTA
ACCGTAAATGAACCTTGTTTTACCGGTCATTTTCCTAGCAGTCCCGTCTT
TCCTGGCGTACTCATTTTAGAAGCCATGGCACAAGCTACAGGCGTTCTAG
CCGTGGCTACATATGGTAAAATGCGTGAAGATGAACTTTATTACTTTGCT
GCAATTGACAATGCACGTTTTAAACGCCCTGTTGTACCAGGTGATCAACT
TGTACTTGAAGTAGAATTTCTAAAAGAAATACGTGGCATTACAAAATTCA
CAGGTAAAGCTTATGTTAATGGTAAATTAGCCTGTGAAGCAGACTTGATG
TGTGCACGTAAATAA


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