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Protein Overview: PANB_ECOLI

General Information:
Name(s) found: PANB_ECOLI [Swiss-Prot]
Description(s) found:
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  • pir||F64736 3-methyl-2-oxobutanoate hydroxymethyltransferase (EC 2.1.2.11) - Escherichia coli (strain K-12) [NCBI NR]
  • gi|400727|sp|P31057.1|PANB_ECOLI RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase; AltName: Full=Ketopantoate hydroxymethyltransferase; Short=KPHMT [NCBI NR]
  • gi|34810450|pdb|1M3U|J Chain J, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [NCBI NR]
  • gi|34810449|pdb|1M3U|I Chain I, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [NCBI NR]
  • gi|34810448|pdb|1M3U|H Chain H, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [NCBI NR]
  • gi|34810447|pdb|1M3U|G Chain G, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [NCBI NR]
  • gi|34810446|pdb|1M3U|F Chain F, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [NCBI NR]
  • gi|34810445|pdb|1M3U|E Chain E, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [NCBI NR]
  • gi|34810444|pdb|1M3U|D Chain D, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [NCBI NR]
  • gi|34810443|pdb|1M3U|C Chain C, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [NCBI NR]
  • gi|34810442|pdb|1M3U|B Chain B, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [NCBI NR]
  • gi|34810441|pdb|1M3U|A Chain A, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [NCBI NR]
  • gi|304927|gb|AAA24271.1| alpha-ketopantoate hydroxymethyl transferase [NCBI NR]
  • gi|21238990|dbj|BAB96711.1| 3-methyl-2-oxobutanoate hydroxymethyltransferase [Escherichia coli W3110] [NCBI NR]
  • 3-methyl-2-oxobutanoate hydroxymethyltransferase (EC 2.1.2.11) (Ketopantoate hydroxymethyltransferase) - Escherichia coli [Swiss-Prot]
  • 3-methyl-2-oxobutanoate hydroxymethyltransferase [Escherichia coli K12]gi|1786326|gb|AAC73245.1| 3-methyl-2-oxobutanoate hydroxymethyltransferase [Escherichia coli K12]gi|34810450|pdb|1M3U|J Chain J, Crystal Structure Of Ketopantoate Hydroxymethyltransf [nrdb_11152004_Chlamydomonas]
  • 3-methyl-2-oxobutanoate hydroxymethyltransferase (Ketopantoate hydroxymethyltransferase) (KPHMT) [NCBI-RefSeq_human_na_08-09-2006_reversed.fasta]
  • Chain H, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [nr-271106-contam.fasta]
  • Chain E, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [nr-271106-contam.fasta]
  • Chain D, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [nr-271106-contam.fasta]
  • Chain C, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [nr-271106-contam.fasta]
  • Chain I, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [nr-271106-contam.fasta]
  • Chain A, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [nr-271106-contam.fasta]
  • Chain G, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [nr-271106-contam.fasta]
  • Chain B, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [nr-271106-contam.fasta]
  • Chain F, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [nr-271106-contam.fasta]
  • Chain J, Crystal Structure Of Ketopantoate Hydroxymethyltransferase Complexed The Product Ketopantoate [nr-271106-contam.fasta]
  • 3-methyl-2-oxobutanoate hydroxymethyltransferase OS=Escherichia coli (strain K12) GN=panB PE=1 SV=1 [uniprot-Ecoli-reviewed-110511.fasta]
    • Organism: Escherichia coli
    Length: 264 amino acids

    Gene Ontology:
    Cellular Component: NONE FOUND
    Biological Process: NONE FOUND
    Molecular Function: NONE FOUND


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MKPTTISLLQ KYKQEKKRFA TITAYDYSFA KLFADEGLNV MLVGDSLGMT VQGHDSTLPV  60
   61 TVADIAYHTA AVRRGAPNCL LLADLPFMAY ATPEQAFENA ATVMRAGANM VKIEGGEWLV 120
  121 ETVQMLTERA VPVCGHLGLT PQSVNIFGGY KVQGRGDEAG DQLLSDALAL EAAGAQLLVL 180
  181 ECVPVELAKR ITEALAIPVI GIGAGNVTDG QILVMHDAFG ITGGHIPKFA KNFLAETGDI 240
  241 RAAVRQYMAE VESGVYPGEE HSFH

    Protein Complex Data

      PUBLICATION TOPOLOGY COCOMPLEXED PROTEINS
    View Details Noble WS, et al. (2009) Manuscript in preparation. PANB_ECOLI gi|189095939, gi...

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

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    No microscopy data found in the PDR for this protein.

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..264] PSI-BLAST 90.69897 Ketopantoate hydroxymethyltransferase PanB

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • 3-methyl-2-oxobutanoate hydroxymethyltransferase activity
    		•  4.08693637310631 bayes_pls_golite062009
  • catalytic activity
    		•  2.59838799615646 bayes_pls_golite062009
  • hydroxymethyl-, formyl- and related transferase activity
    		•  2.05689968523792 bayes_pls_golite062009
  • transferase activity
    		•  1.07154136609184 bayes_pls_golite062009
  • glycine hydroxymethyltransferase activity
    		•  0.646649320021871 bayes_pls_golite062009
  • transferase activity, transferring phosphorus-containing groups
    		•  0.366715189574293 bayes_pls_golite062009
  • oxo-acid-lyase activity
    		•  0.0960362356555544 bayes_pls_golite062009
  • carbon-carbon lyase activity
    		•  0.0846611486307003 bayes_pls_golite062009


    Reference: Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16


    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.96

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle