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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR278 IGR277 IGR276 IGR279 IGR274 IGR280 IGR273 IGR275 orfG, - HD0378 HD0376 nqrE, - HD0383 nqrD, - HD0382 nqrC, - HD0381 add, - HD0377 apbE, - HD0386 nqrF, - HD0384 nqrB, - HD0380 nqrA, - HD0379 orfG, - HD0378 HD0376 nqrE, - HD0383 nqrD, - HD0382 nqrC, - HD0381 add, - HD0377 apbE, - HD0386 nqrF, - HD0384 nqrB, - HD0380 nqrA, - HD0379 orfG, - HD0378 HD0376 nqrE, - HD0383 nqrD, - HD0382 nqrC, - HD0381 add, - HD0377 apbE, - HD0386 nqrF, - HD0384 nqrB, - HD0380 nqrA, - HD0379
* Calculated from Protein Sequence

Gene ID: HD0380

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
nqrB  

Definition:
Na(+)-translocating NADH-quinone reductase subunit B

Gene Start:
299975

Gene Stop:
301207

Gene Length:
1233

Molecular Weight*:
44696

pI*:
9.70

Net Charge*:
5.63

EC:
1.6.5.3  

Functional Class:
Biosynthesis of cofactors, prosthetic groups, and carriers; Menaquinone and ubiquinone  

Pathway: pathway table
Oxidative phosphorylation
Ubiquinone biosynthesis

Secondary Evidence:
Hayashi M, Shibata N, Nakayama Y, Yoshikawa K, Unemoto T.
Korormicin insensitivity in Vibrio alginolyticus is correlated with a single point mutation of Gly-140 in the NqrB subunit of the Na(+)-translocating NADH-quinone reductase.
Arch Biochem Biophys. 2002 May 15;401(2):173-7.
PMID: 12054467

Barquera B, Hellwig P, Zhou W, Morgan JE, Hase CC, Gosink KK, Nilges M, Bruesehoff PJ, Roth A, Lancaster CR, Gennis RB.
Purification and characterization of the recombinant Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae.
Biochemistry. 2002 Mar 19;41(11):3781-9.
PMID: 11888296


Barquera B, Hase CC, Gennis RB.
Expression and mutagenesis of the NqrC subunit of the NQR respiratory Na(+) pump from Vibrio cholerae with covalently attached FMN.
FEBS Lett. 2001 Mar 9;492(1-2):45-9.
PMID: 11248234

Hayashi M, Nakayama Y, Unemoto T.
Recent progress in the Na(+)-translocating NADH-quinone reductase from the marine Vibrio alginolyticus.
Biochim Biophys Acta. 2001 May 1;1505(1):37-44. Review.
PMID: 11248187

Comment:
From GenBank (gi:15214142): The NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinal by two successive reactions, coupled with the transport of NA(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NQRF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one electron transfer pathway. The NQR complex located in the inner membrane (potential) and is composed of six subunits NqrA, NqrB, NqrC, NqrD, NqrE, and NqrF.

From GenBank (gi:6093529): NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.


Blast Summary:  PSI-Blast Search
Residues 1 to 408 are 76% ( EScore : 0.0 ) identical to pir||C64052 NADH dehydrogenase between residues 1 and 408 in [Haemophilus influenzae Rd]
Residues 1 to 408 are 75% ( EScore : 0.0 ) identical to dbj|BAA22911.1| (AB008030) Nqr2 subunit of Na-translocating NADH-quinone reductase complex between residues 1 and 411 in [Vibrio alginolyticus]
Residues 1 to 408 are 75% ( EScore : 0.0 ) identical to gb|AAF95438.1| (AE004300) NADH:ubiquinone oxidoreductase, Na translocating, hydrophobic membrane protein NqrB between residues 13 and 423 in [Vibrio cholerae]
Residues 1 to 408 are 75% ( EScore : 0.0 ) identical to gb|AAD29963.1|AF117331_2 NqrB between residues 1 and 411 in [Vibrio cholerae]
Residues 1 to 409 are 76% ( EScore : 0.0 ) identical to gb|AAF40996.1| (AE002412) Na between residues 1 and 408 in [Neisseria meningitidis MC58]
Residues 1 to 408 are 74% ( EScore : 0.0 ) identical to pir||S51016 NADH dehydrogenase between residues 13 and 423 in [Vibrio alginolyticus]
Residues 1 to 409 are 76% ( EScore : 0.0 ) identical to emb|CAB84034.1| (AL162754) putative Na between residues 1 and 408 in [Neisseria meningitidis]
Residues 3 to 408 are 74% ( EScore : 0.0 ) identical to gb|AAF15412.1|AF165980_2 NqrB between residues 2 and 410 in [Vibrio harveyi]
Residues 14 to 405 are 33% ( EScore : 2e-63 ) identical to gb|AAF39389.1| (AE002323) NADH:ubiquinone oxidoreductase, subunit B, putative between residues 12 and 502 in [Chlamydia muridarum]
Residues 19 to 405 are 30% ( EScore : 3e-55 ) identical to pir||C71535 probable NADH between residues 17 and 502 in [Chlamydia trachomatis]

COGS Summary:  COGS Search
BeTs to 3 clades of COG1805
COG name: Uncharacterized membrane protein, RnfD family
Functional Class: S
The phylogenetic pattern of COG1805 is ------vce--H------in-
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
No significant hits to the Blocks database.

ProDom Summary:  Protein Domain Search
Residues 117-394 are 89% similar to a (COMPLETE PROTEOME UBIQUINONE SUBUNIT) protein domain (PD014218) which is seen in Q9CLB0_PASMU.

Residues 1-79 are 78% similar to a (UBIQUINONE COMPLETE PROTEOME) protein domain (PD041489) which is seen in O05011_HAEIN.



Paralogs:  Local Blast Search
HD0380 is paralogously related to HD0400 (7e-27).


Pfam Summary:  Pfam Search
Residues 38 to 405 (E-value = 1.6e-202) place HD0380 in the NQR2_RnfD_RnfE family which is described as NQR2, RnfD, RnfE family (PF03116)

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

Gene Protein Sequence:
MGLKNLFEKMEPAFHKGGKYEKWYTLFEATYTILYTPGTVTKKDSHVRDA
LDSKRMMILVWLALFPAMFWGMYNVGGQAILATSHLGSLTDSIANNWHYA
FSEAVGATLTADAGWGSKMLLGATYFLPIYLTIFLVGGFWEVVFAMVRKH
EINEGFFVTSILLALIVPPTLPLWQAALAATFGVVVAKEVFGGVGKNFMN
PALAGRAFLFFAYPAQISGDLVWTAADGFSGATALSQWAQGGQIALKHAV
TGQEITWMDAFLGNIPGSIGEVSTLMLMIGAAIIVFARIASWRIIAGVLV
GMAATATLFNLIGSETNLLFAMPWYWHLVLGGFALGMFFMATDPVSASFT
NKGKWWYGALIGVMCVVIRVANPAYPEGMMLAILFANLFAPIFDYLVVQS
NIKRRKAKAA$

Gene Nucleotide Sequence:  Sequence Viewer
ATGGGTTTAAAAAATCTTTTTGAAAAGATGGAACCTGCGTTTCACAAAGG
TGGAAAGTATGAAAAATGGTACACGCTTTTTGAAGCCACATATACTATTC
TTTATACACCGGGTACAGTGACTAAAAAAGACTCGCATGTACGTGATGCG
TTAGATTCTAAGCGAATGATGATTCTCGTATGGTTAGCGTTATTTCCAGC
CATGTTCTGGGGAATGTATAACGTCGGTGGACAAGCTATTCTTGCTACAA
GCCATCTAGGTTCATTAACAGATTCAATTGCAAATAACTGGCATTATGCT
TTCTCCGAGGCTGTGGGGGCTACATTAACTGCTGATGCAGGTTGGGGAAG
CAAAATGTTGCTAGGCGCAACCTATTTCTTACCAATCTATTTAACTATCT
TTTTAGTTGGTGGTTTTTGGGAAGTTGTCTTTGCGATGGTTCGTAAGCAT
GAAATTAATGAAGGCTTTTTTGTTACCTCAATATTATTAGCATTAATCGT
GCCACCTACATTGCCATTATGGCAAGCGGCGTTAGCGGCTACTTTTGGTG
TCGTGGTCGCAAAAGAAGTATTTGGTGGTGTGGGTAAAAACTTTATGAAT
CCTGCGCTTGCGGGGCGTGCGTTTTTATTCTTTGCTTATCCTGCACAGAT
TTCGGGTGATTTAGTATGGACAGCCGCTGATGGTTTTTCAGGCGCAACTG
CACTTTCACAATGGGCACAAGGTGGCCAAATTGCACTTAAGCATGCAGTA
ACCGGTCAAGAAATCACTTGGATGGATGCTTTCTTGGGGAATATTCCTGG
CTCTATCGGTGAGGTTTCTACCTTAATGTTGATGATCGGTGCGGCAATTA
TTGTATTTGCTCGTATTGCATCTTGGCGTATTATCGCCGGTGTGTTAGTC
GGTATGGCTGCAACGGCAACCTTATTTAATTTAATCGGTTCAGAAACAAA
CCTATTATTTGCAATGCCGTGGTATTGGCACTTAGTGTTGGGTGGTTTTG
CACTAGGTATGTTCTTTATGGCGACTGACCCTGTGTCTGCTTCGTTTACC
AATAAAGGTAAATGGTGGTATGGCGCTTTGATTGGGGTAATGTGCGTGGT
TATTCGAGTAGCGAATCCAGCATATCCAGAGGGTATGATGTTAGCAATTT
TATTCGCTAACTTGTTTGCTCCTATCTTTGACTATTTAGTTGTTCAAAGC
AATATCAAACGTAGAAAGGCAAAGGCGGCATAA


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