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Ureaplasma urealyticum Search Results

Record: 1 of 1  
MiniMap tRNA-Trp-2 IGR443 IGR448 IGR446 IGR449 IGR445 IGR450 IGR447 IGR444 rpL33,rpmG, - UU533 cdd, - UU531 pepP,ampP, - UU532 dcm, - UU528 manB,cpsG, - UU530 thrS,syt, - UU534 UU527 codV, - UU529 UU535 rpL33,rpmG, - UU533 cdd, - UU531 pepP,ampP, - UU532 dcm, - UU528 manB,cpsG, - UU530 thrS,syt, - UU534 UU527 codV, - UU529 UU535 Type: tandem, Name:  - 323 Type: tandem, Name:  - 324 Type: tandem, Name:  - 325 rpL33,rpmG, - UU533 cdd, - UU531 pepP,ampP, - UU532 dcm, - UU528 manB,cpsG, - UU530 thrS,syt, - UU534 UU527 codV, - UU529 UU535
* Calculated from Protein Sequence

Gene ID: UU530

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
manB  cpsG  

Definition:
phosphomannomutase

Gene Start:
660407

Gene Stop:
658749

Gene Length:
1659

Molecular Weight*:
64299

pI*:
5.30

Net Charge*:
-12.49

EC:
5.4.2.8  

Functional Class:
central intermediary metabolism; polysaccharides  
energy metabolism; starch and sucrose metabolism  

Pathway: pathway table
Fructose and mannose metabolism

Comment:
Phosphomannomutase converts mannose-1-phosphate to
mannose-6-phosphate.

See Prosite PDOC00589.

From Prosite:

- Phosphomannomutase (EC 5.4.2.8) (PMM). PMM is an enzyme responsible for the conversion of D-mannose 1-phosphate into D-mannose 6-phosphate. PMM is required for different biosynthetic pathways in bacteria. For example, in enterobacteria such as Escherichia coli there are two different genes coding for this enzyme: rfbK which is involved in the synthesis of the O antigen of lipopolysaccharide and cpsG which is required for the synthesis of the M antigen capsular polysaccharide. In Pseudomonas aeruginosa PMM (gene algC) is involved in the biosynthesis of the alginate layer and in Xanthomonas campestris (gene xanA) it is involved in the biosynthesis of xanthan. In Rhizobium strain ngr234 (gene noeK) it is involved in the biosynthesis of the nod factor.


Blast Summary:  PSI-Blast Search
Several significant hits in gapped BLAST to phosphomannomutases; e.g. residues 5-552 are 38% similar to MANB_MYCPI; residues 11-552 are 34% similar to MANB_MYCPN; and residues 19-531 are 26% similar to gi;2688773 (AE001181), the cpsG gene of B.burgdorferi.
BLAST reveals similarity to MG053, TP0642, and CT295, all of which are predicted phosphomannomutases.

COGS Summary:  COGS Search
The phylogenetic pattern of COG0033 is EHgpCMYU.
Cog name: Phosphglucomutase/phosphomannomutase.
Functional class: G.
BeTs to -h-pcmyu.
Number of proteins in this genome belonging to this COG is 1



Blocks Summary:  Blocks Search
Residues 141-155 are in the 100th percentile of similarity to block BL00710 (Phosphoglucomutase and phosphomannomutase phosphoserine signal.)

ProDom Summary:  Protein Domain Search
Residues 179-393 are 41% similar, and residues 394-521 are 39% similar to a defined domain of MANB_MYCPI.
Residues 5-94 are 35% similar to a defined domain of YM8L_YEAST, a phophomannomutase sequence.

Paralogs:  Local Blast Search
No paralogs in U.u.

Pfam Summary:  Pfam Search
Residues 42 to 185 (E-value = 1.5e-49) place UU530 in the PGM_PMM_I family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I (PF02878)

PDB Hit:
gi|1310948|pdb|3PMG|A Chain A, Phosphoglucomutase Mol_id: 1; Molecule: Alpha-D-Glucose-1,6-Bisphosphate; Chain: A, B; Synonym: Phosphoglucomutase; Ec: 5.4.2.2; Heterogen: Mg

Gene Protein Sequence:
MENTNKIFNCWLNSPKIPQVIKEEYKNKTQKEIDHIFDENYRFKFGTSGV
RCIYEEGTRYLNAITYTQLTLGFIEYLETKKNFNKIIVIGRDNRFGSREN
LKLVAEIFSSFDYTVYINEDYGMLSTPITSFLINQLQAGAGIMITASHNP
KNYNGFKVYNANGAQPLVDDTNLIESLMPSYTEALDFNFEFKQDNIRFLT
KEQIQSYFDAVKAQLINTDPNIKKPFKIVFSGHHGTTTKDMIPFLESLGY
DMVSVSEQNFEDPNFNDDPSSNPEEQCSFDLSVEYADNTNAEIMIASDPD
GDRMAIAVRHENYWKFLTGNQTGVLIAHYLLEHKKFTKPTYIISTFISTR
YPELFAKNFDCDVLYVDVGFKNHGNLIANRKKTHNLVVGFEEAIGSLPSD
INNDKDSYQTASILLEMINYYYEQKLDLFTVLKKEIFAKYGNWYSKTTQF
VIDGDNWKQKALIILNNLRNFEFKTVTQYTIHNIIFHEQGSYLEWKLDEY
STIKFRLSGTEPKFKVYIDLYDFSKDQKRDFYQELKIKAEDILDFLKNYL
GL$

Gene Nucleotide Sequence:  Sequence Viewer
ATGGAAAATACAAATAAAATTTTTAATTGTTGATTAAATTCACCAAAAAT
TCCTCAAGTAATTAAAGAAGAATATAAGAATAAAACTCAAAAAGAAATTG
ATCATATTTTTGATGAAAATTATCGATTTAAATTCGGTACATCAGGTGTA
CGTTGTATTTATGAAGAAGGAACTCGTTATTTAAATGCAATAACTTATAC
TCAATTGACATTAGGTTTTATTGAATATTTAGAAACGAAAAAGAATTTTA
ATAAAATTATTGTTATTGGCCGAGACAACCGCTTTGGCTCACGTGAAAAT
TTGAAACTAGTTGCTGAAATTTTTAGTAGTTTTGATTATACTGTTTATAT
TAATGAAGATTATGGGATGTTATCAACTCCAATTACTTCATTTTTAATTA
ATCAATTACAAGCAGGAGCTGGAATTATGATCACCGCTTCTCATAATCCT
AAAAATTATAATGGTTTTAAAGTTTATAATGCTAATGGTGCTCAGCCATT
AGTTGATGATACTAATCTCATTGAATCTTTAATGCCATCATATACAGAAG
CATTGGATTTTAACTTTGAATTTAAACAAGATAATATTAGATTTTTAACA
AAAGAACAAATTCAAAGTTATTTTGATGCAGTTAAAGCACAACTAATTAA
TACTGATCCTAATATTAAAAAACCCTTCAAAATTGTTTTTAGTGGTCATC
ATGGAACAACAACAAAGGACATGATTCCTTTTTTAGAATCACTTGGTTAT
GATATGGTTAGCGTTAGCGAACAAAATTTTGAAGATCCTAATTTTAATGA
TGACCCAAGTTCTAATCCAGAAGAACAATGTTCATTTGATTTAAGTGTTG
AATATGCAGACAATACAAACGCAGAAATAATGATTGCATCTGATCCTGAT
GGAGATCGAATGGCCATTGCTGTACGTCATGAAAATTATTGAAAATTTTT
GACTGGTAATCAAACAGGTGTTTTAATTGCGCATTATTTATTAGAACATA
AAAAATTTACTAAACCTACATATATTATTTCAACATTTATTTCAACACGC
TATCCAGAATTATTTGCTAAAAATTTTGATTGTGATGTTTTATATGTAGA
TGTAGGTTTTAAAAATCATGGTAATTTAATTGCCAATCGTAAAAAAACAC
ATAATTTGGTTGTTGGTTTTGAAGAAGCAATTGGTTCATTACCATCTGAT
ATTAATAATGATAAAGATTCATATCAAACTGCGTCTATTTTGTTAGAAAT
GATTAATTATTATTATGAACAAAAACTTGATTTATTTACCGTTTTAAAAA
AAGAGATTTTTGCTAAGTATGGGAATTGATATAGTAAAACTACTCAGTTT
GTTATTGATGGTGATAACTGAAAACAAAAAGCACTTATTATTTTAAATAA
CTTAAGAAATTTTGAATTTAAAACAGTAACCCAATACACCATTCATAACA
TTATTTTTCATGAACAAGGATCTTATCTTGAATGAAAATTAGACGAATAC
TCAACAATCAAATTTAGATTATCTGGAACAGAACCTAAATTTAAAGTATA
TATTGATTTATATGATTTTAGCAAAGATCAAAAACGAGATTTTTATCAAG
AACTAAAAATTAAAGCTGAAGATATTTTAGATTTTTTAAAAAATTATTTA
GGTCTTTAA


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