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1:  NP_843066Reports  glutamate-1-semia...[gi:30260689] BLink, Conserved Domains, Links
LOCUS       NP_843066                434 aa            linear   BCT 20-JUL-2008
DEFINITION  glutamate-1-semialdehyde aminotransferase [Bacillus anthracis str.
            Ames].
ACCESSION   NP_843066
VERSION     NP_843066.1  GI:30260689
DBSOURCE    REFSEQ: accession NC_003997.3
KEYWORDS    .
SOURCE      Bacillus anthracis str. Ames
  ORGANISM  Bacillus anthracis str. Ames
            Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus
            cereus group.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Read,T., Peterson,S., Tourasse,N., Baillie,L., Paulsen,I.,
            Nelson,K., Tettelin,H., Fouts,D., Eisen,J., Gill,S., Holtzapple,E.,
            Okstad,O., Helgason,E., Rilstone,J., Wu,M., Kolonay,J., Beanan,M.,
            Dodson,R., Brinkac,L., Gwinn,M., DeBoy,R., Madupu,R., Daugherty,S.,
            Durkin,A., Haft,D., Nelson,W., Peterson,J., Pop,M., Khouri,H.,
            Radune,D., Benton,J., Mahamoud,Y., Jiang,L., Hance,I., Weidman,J.,
            Berry,K., Plaut,R., Wolf,A., Watkins,K., Nierman,W., Hazen,A.,
            Cline,R., Redmond,C., Thwaite,J., White,O., Salzberg,S.,
            Thomason,B., Friedlander,A., Koehler,T., Hanna,P., Kolsto,A.-B. and
            Fraser,C.
  TITLE     The genome sequence of Bacillus anthracis Ames and comparison to
            closely related bacteria
  JOURNAL   Nature 423 (6935), 81-86 (2003)
   PUBMED   12721629
REFERENCE   2  (residues 1 to 434)
  CONSRTM   NCBI Genome Project
  TITLE     Direct Submission
  JOURNAL   Submitted (10-SEP-2004) National Center for Biotechnology
            Information, NIH, Bethesda, MD 20894, USA
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Read,T., Peterson,S., Tourasse,N., Baillie,L., Paulsen,I.,
            Nelson,K., Tettelin,H., Fouts,D., Eisen,J., Gill,S., Holtzapple,E.,
            Okstad,O., Helgason,E., Rilstone,J., Wu,M., Kolonay,J., Beanan,M.,
            Dodson,R., Brinkac,L., Gwinn,M., DeBoy,R., Madupu,R., Daugherty,S.,
            Durkin,A., Haft,D., Nelson,W., Peterson,J., Pop,M., Khouri,H.,
            Radune,D., Benton,J., Mahamoud,Y., Jiang,L., Hance,I., Weidman,J.,
            Berry,K., Plaut,R., Wolf,A., Watkins,K., Nierman,W., Hazen,A.,
            Cline,R., Redmond,C., Thwaite,J., White,O., Salzberg,S.,
            Thomason,B., Friedlander,A., Koehler,T., Hanna,P., Kolsto,A.-B. and
            Fraser,C.
  TITLE     Direct Submission
  JOURNAL   Submitted (26-MAR-2003) The Institute for Genomic Research, 9712
            Medical Center Dr, Rockville, MD 20850, USA
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AAP24552.
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Bacillus anthracis str. Ames"
                     /strain="Ames"
                     /db_xref="taxon:198094"
     Protein         1..434
                     /product="glutamate-1-semialdehyde aminotransferase"
                     /EC_number="5.4.3.8"
                     /calculated_mol_wt=46301
     Region          2..431
                     /region_name="HemL"
                     /note="Glutamate-1-semialdehyde aminotransferase [Coenzyme
                     metabolism]; COG0001"
                     /db_xref="CDD:30350"
     Region          11..427
                     /region_name="OAT_like"
                     /note="Acetyl ornithine aminotransferase family. This
                     family belongs to pyridoxal phosphate (PLP)-dependent
                     aspartate aminotransferase superfamily (fold I). The major
                     groups in this CD correspond to ornithine
                     aminotransferase, acetylornithine aminotransferase...;
                     cd00610"
                     /db_xref="CDD:99735"
     Site            order(119..121,147..148,150,209,242,244..245,270)
                     /site_type="inhibition"
                     /note="inhibitor-cofactor binding pocket"
                     /db_xref="CDD:99735"
     Site            order(120..121,147..148,209,242,245,270)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site"
                     /db_xref="CDD:99735"
     Site            270
                     /site_type="other"
                     /note="catalytic residue"
                     /db_xref="CDD:99735"
     CDS             1..434
                     /gene="hemL-1"
                     /locus_tag="BA0531"
                     /coded_by="complement(NC_003997.3:525778..527082)"
                     /note="converts (S)-4-amino-5-oxopentanoate to
                     5-aminolevulinate"
                     /transl_table=11
                     /db_xref="GeneID:1087796"
ORIGIN      
        1 mvvkftksea lhkealehiv ggvnspsrsf kavgggapia mergkgayfw dvdgnkyidy
       61 laaygpiitg hahphitkai ttaaengvly gtptalevkf akmlkeampa ldkvrfvnsg
      121 teavmttirv araytgrtki mkfagcyhgh sdlvlvaags gpstlgtpds agvpqsiaqe
      181 vitvpfnnve tlkealdkwg hevaailvep ivgnfgivep kpgflekvne lvheagalvi
      241 ydevitafrf myggaqdllg vtpdltalgk viggglpiga yggkkeimeq vaplgpayqa
      301 gtmagnpasm asgiaclevl qqeglyekld elgamlekgi leqaakhnid itlnrlkgal
      361 tvyfttntie dydaaqdtdg emfgkffklm lqegvnlaps kyeawfltte htkedieyti
      421 eavgrafaal adnk
//

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Last update: Mon, 12 Jan 2009 Rev. 149544