LOCUS YP_001918204 373 aa linear CON 10-JUN-2013
DEFINITION histidinol-phosphate aminotransferase [Natranaerobius thermophilus
JW/NM-WN-LF].
ACCESSION YP_001918204
VERSION YP_001918204.1 GI:188586659
DBLINK Project: 59001
BioProject: PRJNA59001
DBSOURCE REFSEQ: accession NC_010718.1
KEYWORDS .
SOURCE Natranaerobius thermophilus JW/NM-WN-LF
ORGANISM Natranaerobius thermophilus JW/NM-WN-LF
Bacteria; Firmicutes; Clostridia; Natranaerobiales;
Natranaerobiaceae; Natranaerobius.
REFERENCE 1 (residues 1 to 373)
AUTHORS Zhao,B., Mesbah,N.M., Dalin,E., Goodwin,L., Nolan,M., Pitluck,S.,
Chertkov,O., Brettin,T.S., Han,J., Larimer,F.W., Land,M.L.,
Hauser,L., Kyrpides,N. and Wiegel,J.
TITLE Complete Genome Sequence of the Anaerobic, Halophilic
Alkalithermophile Natranaerobius thermophilus JW/NM-WN-LF
JOURNAL J. Bacteriol. 193 (15), 4023-4024 (2011)
PUBMED 21642468
REFERENCE 2 (residues 1 to 373)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (20-MAY-2008) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 3 (residues 1 to 373)
AUTHORS Copeland,A., Lucas,S., Lapidus,A., Glavina del Rio,T., Dalin,E.,
Tice,H., Bruce,D., Goodwin,L., Pitluck,S., Chertkov,O., Brettin,T.,
Detter,J.C., Han,C., Kuske,C.R., Schmutz,J., Larimer,F., Land,M.,
Hauser,L., Kyrpides,N., Lykidis,A., Mesbah,N.M. and Wiegel,J.
CONSRTM US DOE Joint Genome Institute
TITLE Direct Submission
JOURNAL Submitted (04-APR-2008) 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 was derived from ACB85616.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..373
/organism="Natranaerobius thermophilus JW/NM-WN-LF"
/strain="JW/NM-WN-LF"
/db_xref="taxon:457570"
/note="type strain of Natranaerobius thermophilus"
Protein 1..373
/product="histidinol-phosphate aminotransferase"
/calculated_mol_wt=41720
Region 13..366
/region_name="PRK02731"
/note="histidinol-phosphate aminotransferase; Validated"
/db_xref="CDD:235064"
Region 42..365
/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(98..100,124,171,201,228,230..231,239)
/site_type="other"
/note="pyridoxal 5'-phosphate binding site [chemical
binding]"
/db_xref="CDD:99734"
Site order(101,134,194,237..239,266,269)
/site_type="other"
/note="homodimer interface [polypeptide binding]"
/db_xref="CDD:99734"
Site 231
/site_type="active"
/note="catalytic residue [active]"
/db_xref="CDD:99734"
CDS 1..373
/locus_tag="Nther_2049"
/coded_by="NC_010718.1:2165290..2166411"
/note="TIGRFAM: histidinol-phosphate aminotransferase;
PFAM: aminotransferase class I and II;
KEGG: csc:Csac_2697 histidinol-phosphate aminotransferase"
/transl_table=11
/db_xref="InterPro:IPR004839"
/db_xref="InterPro:IPR005861"
/db_xref="GeneID:6315567"
CONTIG join(WP_012448473.1:1..373)
ORIGIN
1 mgtkktqfpq dsarkvlnef spyipgksle eikekygldk viklasnenp hgpspkavkk
61 ltdnkdihly pqksyqnlqs kisqklgtnp gqviigngsd eiikllaaaf inpgeeglma
121 ditfpiykma vkeldgkvth iplkkythdi dqfiaqitdn tklificnpn nptgsiithe
181 eaekllssvs kdtivvfdea yreyvtnpef pktemlvdky pnlialrtfs kiyglaalrv
241 gygigsekli evlhkvklpf nvnelglraa qealddtehl nyskeqndqg kkwlesklks
301 skffspvpsq anfllvktef daeklagell kqgviiregt sfgmpdhfri tigsksdnef
361 fieklsncev nlk
//