LOCUS YP_004080739 319 aa linear BCT 10-JUN-2013
DEFINITION deoxyribose-phosphate aldolase [Micromonospora sp. L5].
ACCESSION YP_004080739
VERSION YP_004080739.1 GI:315501852
DBLINK Project: 45895
BioProject: PRJNA45895
DBSOURCE REFSEQ: accession NC_014815.1
KEYWORDS .
SOURCE Micromonospora sp. L5
ORGANISM Micromonospora sp. L5
Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
Micromonosporineae; Micromonosporaceae; Micromonospora.
REFERENCE 1 (residues 1 to 319)
AUTHORS Lucas,S., Copeland,A., Lapidus,A., Cheng,J.-F., Bruce,D.,
Goodwin,L., Pitluck,S., Saunders,E., Detter,J.C., Han,C., Tapia,R.,
Land,M., Hauser,L., Jeffries,C., Kyrpides,N., Ivanova,N.,
Ovchinnikova,G., De Hoff,P.L., Hirsch,A.M. and Woyke,T.
CONSRTM US DOE Joint Genome Institute
TITLE Complete sequence of Micromonospora sp. L5
JOURNAL Unpublished
REFERENCE 2 (residues 1 to 319)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (23-DEC-2010) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 3 (residues 1 to 319)
AUTHORS Lucas,S., Copeland,A., Lapidus,A., Cheng,J.-F., Bruce,D.,
Goodwin,L., Pitluck,S., Saunders,E., Detter,J.C., Han,C., Tapia,R.,
Land,M., Hauser,L., Jeffries,C., Kyrpides,N., Ivanova,N.,
Ovchinnikova,G., De Hoff,P.L., Hirsch,A.M. and Woyke,T.
CONSRTM US DOE Joint Genome Institute
TITLE Direct Submission
JOURNAL Submitted (16-DEC-2010) US DOE Joint Genome Institute, 2800
Mitchell Drive B310, 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 ADU06588.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..319
/organism="Micromonospora sp. L5"
/strain="L5"
/db_xref="taxon:648999"
Protein 1..319
/product="deoxyribose-phosphate aldolase"
/EC_number="4.1.2.4"
/calculated_mol_wt=33637
Region 61..292
/region_name="DeoC"
/note="2-deoxyribose-5-phosphate aldolase (DERA) of the
DeoC family; cd00959"
/db_xref="CDD:188646"
Site order(70,72,74,106..108,130,138,143,148..151,160,162,
181..182,196)
/site_type="other"
/note="intersubunit interface [polypeptide binding]"
/db_xref="CDD:188646"
Site order(219,222,257..259,290..292)
/site_type="active"
/db_xref="CDD:188646"
Site 219
/site_type="active"
/note="catalytic residue [active]"
/db_xref="CDD:188646"
CDS 1..319
/locus_tag="ML5_1048"
/coded_by="complement(NC_014815.1:1042395..1043354)"
/inference="protein motif:TFAM:TIGR00126"
/note="TIGRFAM: deoxyribose-phosphate aldolase;
KEGG: saq:Sare_0772 deoxyribose-phosphate aldolase;
PFAM: deoxyribose-phosphate
aldolase/phospho-2-dehydro-3-deoxyheptonate aldolase"
/transl_table=11
/db_xref="GO:0004139"
/db_xref="InterPro:IPR002915"
/db_xref="InterPro:IPR011343"
/db_xref="GeneID:10056538"
ORIGIN
1 mtatttsars dltelgrset alrtflhglp gvdqvgaeqr aaqlgtrsik ttakaeaidl
61 airmvdlttl egadtpgkvr alaakalrpd padpscphvg avcvypsmvp yvaevlrgsg
121 vhlasvataf psgqapleik ladvraavea gadeidmvin rgaflagrys dvydeivatk
181 eacgdahlkv iletgelaty dnvrraswla mlaggdfikt stgkvpvaat lpvtlvmlea
241 vrdfraatgr qvgvkpaggi kttkdaikyl vmvnetvgad wlspdwfrfg assllndllm
301 qrtklttgvy agpdyftld
//