LOCUS YP_001379496 364 aa linear BCT 27-SEP-2012
DEFINITION histidinol-phosphate aminotransferase [Anaeromyxobacter sp.
Fw109-5].
ACCESSION YP_001379496
VERSION YP_001379496.1 GI:153005171
DBLINK Project: 58755
BioProject: PRJNA58755
DBSOURCE REFSEQ: accession NC_009675.1
KEYWORDS .
SOURCE Anaeromyxobacter sp. Fw109-5
ORGANISM Anaeromyxobacter sp. Fw109-5
Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
REFERENCE 1 (residues 1 to 364)
AUTHORS Copeland,A., Lucas,S., Lapidus,A., Barry,K., Glavina del Rio,T.,
Dalin,E., Tice,H., Pitluck,S., Sims,D., Brettin,T., Bruce,D.,
Detter,J.C., Han,C., Schmutz,J., Larimer,F., Land,M., Hauser,L.,
Kyrpides,N., Lykidis,A., Fields,M. and Richardson,P.
CONSRTM US DOE Joint Genome Institute
TITLE Complete sequence of Anaeromyxobacter sp. Fw109-5
JOURNAL Unpublished
REFERENCE 2 (residues 1 to 364)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (24-JUL-2007) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 3 (residues 1 to 364)
AUTHORS Copeland,A., Lucas,S., Lapidus,A., Barry,K., Glavina del Rio,T.,
Dalin,E., Tice,H., Pitluck,S., Sims,D., Brettin,T., Bruce,D.,
Detter,J.C., Han,C., Schmutz,J., Larimer,F., Land,M., Hauser,L.,
Kyrpides,N., Lykidis,A., Fields,M. and Richardson,P.
CONSRTM US DOE Joint Genome Institute
TITLE Direct Submission
JOURNAL Submitted (12-JUL-2007) US DOE Joint Genome Institute, 2800
Mitchell Drive B100, Walnut Creek, CA 94598-1698, USA
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence is identical to ABS26512.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..364
/organism="Anaeromyxobacter sp. Fw109-5"
/strain="Fw109-5"
/db_xref="taxon:404589"
Protein 1..364
/product="histidinol-phosphate aminotransferase"
/calculated_mol_wt=39100
Region 1..364
/region_name="PRK02731"
/note="histidinol-phosphate aminotransferase; Validated"
/db_xref="CDD:179465"
Region 60..360
/region_name="AAT_like"
/note="Aspartate aminotransferase family. This family
belongs to pyridoxal phosphate (PLP)-dependent aspartate
aminotransferase superfamily (fold I). Pyridoxal phosphate
combines with an alpha-amino acid to form a compound
called a Schiff base or aldimine...; cd00609"
/db_xref="CDD:99734"
Site order(90..92,116,164,194,221,223..224,232)
/site_type="other"
/note="pyridoxal 5'-phosphate binding site [chemical
binding]"
/db_xref="CDD:99734"
Site order(93,126,187,230..232,258,261)
/site_type="other"
/note="homodimer interface [polypeptide binding]"
/db_xref="CDD:99734"
Site 224
/site_type="active"
/note="catalytic residue [active]"
/db_xref="CDD:99734"
CDS 1..364
/locus_tag="Anae109_2310"
/coded_by="complement(NC_009675.1:2614757..2615851)"
/note="catalyzes the formation of L-histidinol phosphate
from imidazole-acetol phosphate and glutamate in histidine
biosynthesis"
/transl_table=11
/db_xref="InterPro:IPR004839"
/db_xref="InterPro:IPR005861"
/db_xref="GeneID:5378048"
ORIGIN
1 mplvpphvas ltpyvpgkpi eevereygvs nvaklasnen algpsplala aareacakvh
61 lypdgsayll rnaiaaklgv ppeevmvgng sneliellvr tfvldgeevl tsaqsfvayk
121 laahehgrtl veapmkgrfh ydldalrkll srrtklvfla npdnptgtwf teaeltpfld
181 avpkdtlvvl deayveyvda pgfqdglalr rkypnvvvlr tfskiyglag mrlgyglarp
241 evveyvdrvr ppfntnlvaq aagaaalgds ahvaksralv leerpflakg laalgaivvp
301 sqgnfvladf pgrtgkdlfe allregviar pvagygfpsa lritvglrre nerclaalgr
361 ilga
//