LOCUS YP_001314703 249 aa linear BCT 25-JAN-2012
DEFINITION carbonate dehydratase [Sinorhizobium medicae WSM419].
ACCESSION YP_001314703
VERSION YP_001314703.1 GI:150378108
DBLINK Project: 58549
BioProject: PRJNA58549
DBSOURCE REFSEQ: accession NC_009621.1
KEYWORDS .
SOURCE Sinorhizobium medicae WSM419
ORGANISM Sinorhizobium medicae WSM419
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
REFERENCE 1 (residues 1 to 249)
AUTHORS Reeve,W., Chain,P., O'Hara,G., Ardley,J., Nandesena,K., Brau,L.,
Tiwari,R., Malfatti,S., Kiss,H., Lapidus,A., Copeland,A., Nolan,M.,
Land,M., Hauser,L., Chang,Y.J., Ivanova,N., Mavromatis,K.,
Markowitz,V., Kyrpides,N., Gollagher,M., Yates,R., Dilworth,M. and
Howieson,J.
TITLE Complete genome sequence of the Medicago microsymbiont Ensifer
(Sinorhizobium) medicae strain WSM419
JOURNAL Stand Genomic Sci 2 (1), 77-86 (2010)
PUBMED 21304680
REMARK Publication Status: Online-Only
REFERENCE 2 (residues 1 to 249)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (03-JUL-2007) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 3 (residues 1 to 249)
AUTHORS Copeland,A., Lucas,S., Lapidus,A., Barry,K., Glavina del Rio,T.,
Dalin,E., Tice,H., Pitluck,S., Chain,P., Malfatti,S., Shin,M.,
Vergez,L., Schmutz,J., Larimer,F., Land,M., Hauser,L., Kyrpides,N.,
Mikhailova,N., Reeve,W. and Richardson,P.
CONSRTM US DOE Joint Genome Institute
TITLE Direct Submission
JOURNAL Submitted (21-JUN-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 was derived from ABR64770.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..249
/organism="Sinorhizobium medicae WSM419"
/strain="WSM419"
/db_xref="taxon:366394"
/plasmid="pSMED02"
Protein 1..249
/product="carbonate dehydratase"
/EC_number="4.2.1.1"
/calculated_mol_wt=24074
Region 1..249
/region_name="Cah"
/note="Carbonic anhydrase [Inorganic ion transport and
metabolism]; COG3338"
/db_xref="CDD:33147"
sig_peptide 1..26
/product="hypothetical protein"
/note="Signal predicted by SignalP 3.0 HMM (Signal peptide
probability 1.000) with cleavage site probability 1.000 at
residue 26"
/calculated_mol_wt=2897
Region 38..247
/region_name="alpha_CA_prokaryotic_like"
/note="Carbonic anhydrase alpha, prokaryotic-like
subfamily. Carbonic anhydrases (CAs) are zinc-containing
enzymes that catalyze the reversible hydration of carbon
dioxide in a two-step mechanism: a nucleophilic attack of
a zinc-bound hydroxide ion on carbon...; cd03124"
/db_xref="CDD:28766"
Site order(89,112,114,116,120,133,200)
/site_type="active"
/db_xref="CDD:28766"
Site order(114,116,133)
/site_type="other"
/note="zinc binding site [ion binding]"
/db_xref="CDD:28766"
CDS 1..249
/locus_tag="Smed_6140"
/coded_by="NC_009621.1:1065775..1066524"
/note="PFAM: carbonic anhydrase;
KEGG: sme:SMa0045 probable carbonic anhydrase, Cah"
/transl_table=11
/db_xref="InterPro:IPR001148"
/db_xref="InterPro:IPR006311"
/db_xref="GeneID:5320442"
ORIGIN
1 merrdfikrl allaacplca etayaaeaeh wsyegeagpe hwgslsnens acsagsqqsp
61 ldirgaikad ipglalnwks ggailnnght iqvkaapggt lrrgdkpyel vqyhfhapse
121 hlveghrfpm evhfvhkhae tgalgvlgvf fvpgaanttf aslaatfpqk tgeqtalpnv
181 dpsgllptsl rywayegslt tppcseivdw miaqdpievd aadidrftal ysmnarpalv
241 anrryilas
//