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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap rRNA-5S-3 IGR440 IGR448 IGR446 IGR439 IGR443 IGR445 IGR444 IGR447 IGR438 IGR442 IGR441 IGR437 HD0641 HD0640 ftsN, - HD0639 mob, - HD0636 HD0637 arsC, - HD0631 aroD,aroQ, - HD0632 accB, - HD0634 por,dsbA, - HD0638 dapD, - HD0630 pqiA, - HD0629 accC, - HD0635 HD0641 HD0640 ftsN, - HD0639 mob, - HD0636 HD0637 arsC, - HD0631 aroD,aroQ, - HD0632 accB, - HD0634 por,dsbA, - HD0638 dapD, - HD0630 pqiA, - HD0629 accC, - HD0635 HD0640 ftsN, - HD0639 mob, - HD0636 HD0641 HD0637 arsC, - HD0631 aroD,aroQ, - HD0632 accB, - HD0634 por,dsbA, - HD0638 dapD, - HD0630 pqiA, - HD0629 accC, - HD0635
* Calculated from Protein Sequence

Gene ID: HD0635

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
accC  

Definition:
biotin carboxylase (subunit of acetyl-CoA carboxylase)

Gene Start:
498719

Gene Stop:
500062

Gene Length:
1344

Molecular Weight*:
49168

pI*:
6.80

Net Charge*:
-1.21

EC:
6.3.4.14  

Functional Class:
Fatty acid and phospholipid metabolism  

Pathway: pathway table
Fatty acid biosynthesis (path 1)

Secondary Evidence:
Kondo,H., Shiratsuchi,K., Yoshimoto,T., Masuda,T., Kitazono,A.,
Tsuru,D., Anai,M., Sekiguchi,M. and Tanabe,T.
Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit
Proc. Natl. Acad. Sci. U.S.A. 88 (21), 9730-9733 (1991)
MEDLINE: 92052166

Li,S.J. and Cronan,J.E. Jr.
The gene encoding the biotin carboxylase subunit of Escherichia
coli acetyl-CoA carboxylase
J. Biol. Chem. 267 (2), 855-863 (1992)
MEDLINE: 92112819

Waldrop,G.L., Rayment,I. and Holden,H.M.
Three-dimensional structure of the biotin carboxylase subunit of
acetyl-CoA carboxylase
Biochemistry 33 (34), 10249-10256 (1994)
MEDLINE: 94347758

Thoden,J.B., Blanchard,C.Z., Holden,H.M. and Waldrop,G.L.
Movement of the biotin carboxylase B-domain as a result of ATP
binding
J. Biol. Chem. 275 (21), 16183-16190 (2000)
MEDLINE: 20283656



Comment:
For other biotin-related genes, see HD0634, HD0082, HD1007, HD1394, HD1480, HD1680, HD1681.

Blast Summary:  PSI-Blast Search
Many very strong hits in gapped BLAST to biotin carboxylase; e.g., residues 26-471 are 86% similar to ACCC_HAEIN [168279], residues 26-472 are 81% similar to ACCC_ECOLI [461457], and residues 26- are 79% similar to the sequence for acetyl-CoA carboxylase, biotin carboxylase in Vibrio cholerae [9654706].
There are also strong hits to pyruvate carboxylase, subunit A; e.g., residues 26-469 are 57% similar to PYCA_METJA [2493313].

COGS Summary:  COGS Search
BeTs to 12 clades of COG0439
COG name: Biotin carboxylase
Functional Class:  I
The phylogenetic pattern of COG0439 is amt-YQ-CeBRhuj----inx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001882 (Biotin-requiring enzymes attachment site) with a combined E-value of 3.9e-96.
    IPB001882A    75-95
    IPB001882B    104-132
    IPB001882C    153-170
    IPB001882D    209-244
    IPB001882E    267-281
    IPB001882F    292-301
    IPB001882G    332-350
***** IPB000901 (Carbamoyl-phosphate synthase) with a combined E-value of 7.4e-18.
    IPB000901    149-172


ProDom Summary:  Protein Domain Search
Residues 59-92 are 91% similar to a (CARBOXYLASE BIOTIN PYRUVATE LIGASE PROTEOME COMPLETE) protein domain (PD371458) which is seen in ACCC_HAEIN.

Residues 292-442 are 85% similar to a (CARBOXYLASE BIOTIN LIGASE ACETYL-COA PYRUVATE PROTEOME) protein domain (PD000755) which is seen in ACCC_HAEIN.

Residues 219-291 are 52% similar to a (CARBOXYLASE BIOTIN PEPTIDE PRECURSOR) protein domain (PD253426) which is seen in O67449_AQUAE.

Residues 96-291 are 85% similar to a (LIGASE SYNTHETASE CARBOXYLASE COMPLETE PROTEOME) protein domain (PD000180) which is seen in Q9CLV9_PASMU.

Residues 2-56 are 98% similar to a (CARBOXYLASE BIOTIN PYRUVATE PROTEOME LIGASE COMPLETE) protein domain (PD000820) which is seen in Q9CLV9_PASMU.



Paralogs:  Local Blast Search

HD0635 is paralogously related to HD0233 (1e-12).


Pfam Summary:  Pfam Search
Residues 1 to 113 (E-value = 3.8e-57) place HD0635 in the CPSase_L_chain family which is described as Carbamoyl-phosphate synthase L chain, N-terminal domain (PF00289)
Residues 115 to 329 (E-value = 1.7e-119) place HD0635 in the CPSase_L_D2 family which is described as Carbamoyl-phosphate synthase L chain, ATP binding domain (PF02786)
Residues 336 to 441 (E-value = 1.6e-64) place HD0635 in the Biotin_carb_C family which is described as Biotin carboxylase C-terminal domain (PF02785)

PDB Hit:
pdb|1DV1|A Chain A, Structure Of Biotin Carboxylase (Apo) >gi|9... 751 0.0
pdb|1DV2|A Chain A, The Structure Of Biotin Carboxylase, Mutant... 749 0.0

Gene Protein Sequence:
MLEKVVIANRGEIALRVLRACKELGIKTVAVHSTADRELKHVLLADETVC
IGPAPSVKSYLNIPMIIAAAEITNADAIHPGYGFLSENADFAEQVEKSGF
TFIGPTADVIRLMGDKVSAIEAMKKAGVPCVPGSDGPIGNDPVKNKEIAN
RIGYPVIIKASGGGGGRGMRVVYQAKDLEASIAMTKAEAKAAFNNDMVYM
EKYLENPRHIEIQVLADTHGNAVYLAERDCSMQRRHQKVVEEAPAPGITP
ELRKFIGERCAKACREIGYRGAGTFEFLFENGEFYFIEMNTRLQVEHPVT
EMITGVDLVKEQLRVAAGLPISIKQEDIKVKGHAMECRINAEDPNTFLPS
PGKITRLHVPGGLGVRWDSHIYSGYTVPPHYDSMIGKLITFAENREIAIR
RMQNALSETILEGIKTNIPLHNLIMEDENFCQGGTNIHYLEKKLGLK$

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTAGAAAAAGTTGTCATAGCAAATCGTGGCGAGATTGCGTTACGTGT
TTTGCGTGCCTGTAAAGAACTAGGCATTAAAACTGTTGCAGTTCATTCAA
CCGCGGACCGAGAATTAAAGCACGTTTTACTTGCAGATGAAACCGTCTGT
ATTGGTCCCGCTCCTTCTGTGAAAAGTTATTTAAATATTCCTATGATTAT
TGCTGCGGCAGAAATTACTAACGCAGATGCAATTCACCCCGGTTATGGGT
TCTTATCTGAAAATGCTGATTTTGCAGAGCAAGTTGAAAAATCAGGTTTT
ACGTTTATTGGCCCAACGGCAGATGTGATTCGACTAATGGGCGATAAAGT
TTCTGCTATTGAAGCCATGAAAAAAGCAGGGGTGCCTTGTGTGCCGGGTT
CAGATGGGCCTATTGGTAATGATCCTGTTAAAAATAAAGAGATTGCTAAC
CGCATTGGTTATCCTGTGATTATCAAAGCATCTGGTGGTGGCGGTGGTCG
TGGTATGCGCGTGGTTTATCAAGCAAAAGATTTAGAAGCATCTATTGCTA
TGACGAAAGCAGAGGCGAAAGCAGCCTTTAATAATGATATGGTGTATATG
GAAAAATATTTAGAAAATCCGCGCCATATTGAGATTCAAGTGCTAGCAGA
TACACACGGTAATGCTGTTTATTTAGCTGAACGTGATTGCTCAATGCAAC
GTCGCCATCAGAAAGTTGTTGAAGAAGCGCCTGCGCCGGGGATTACACCT
GAATTACGTAAGTTTATTGGTGAGCGCTGTGCGAAGGCTTGTCGTGAAAT
TGGTTATCGTGGTGCGGGCACTTTTGAGTTCTTATTTGAGAACGGTGAAT
TTTACTTTATTGAGATGAACACGCGTTTGCAAGTAGAACATCCGGTTACT
GAAATGATTACAGGAGTCGATTTAGTTAAAGAACAGTTACGTGTTGCGGC
AGGTTTACCGATTTCAATTAAGCAAGAAGATATCAAGGTAAAAGGTCATG
CTATGGAATGCCGTATTAATGCGGAGGATCCAAATACTTTCTTACCATCA
CCGGGTAAGATCACGCGTTTACATGTTCCAGGTGGATTAGGTGTGCGTTG
GGATTCACATATTTATTCTGGTTATACTGTGCCGCCTCACTATGATTCAA
TGATTGGTAAGTTGATTACGTTTGCTGAAAATCGTGAAATTGCTATTCGT
CGTATGCAAAATGCGCTATCTGAAACGATTTTAGAAGGCATTAAAACGAA
TATTCCATTGCATAATTTAATTATGGAAGATGAGAATTTCTGCCAAGGTG
GGACTAATATTCATTATCTTGAAAAGAAATTAGGTCTCAAATAA


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