(data stored in SCRATCH zone)

SWISSPROT: C5BDL1_EDWI9

ID   C5BDL1_EDWI9            Unreviewed;       342 AA.
AC   C5BDL1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 48.
DE   SubName: Full=KamA family protein {ECO:0000313|EMBL:ACR67627.1};
GN   OrderedLocusNames=NT01EI_0386 {ECO:0000313|EMBL:ACR67627.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67627.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR603739-50};
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DR   EMBL; CP001600; ACR67627.1; -; Genomic_DNA.
DR   RefSeq; WP_015869833.1; NC_012779.2.
DR   ProteinModelPortal; C5BDL1; -.
DR   STRING; 634503.NT01EI_0386; -.
DR   EnsemblBacteria; ACR67627; ACR67627; NT01EI_0386.
DR   GeneID; 7960166; -.
DR   KEGG; eic:NT01EI_0386; -.
DR   PATRIC; fig|634503.3.peg.350; -.
DR   eggNOG; ENOG4105CK3; Bacteria.
DR   eggNOG; COG1509; LUCA.
DR   HOGENOM; HOG000223517; -.
DR   KO; K19810; -.
DR   OMA; PIWLNTH; -.
DR   OrthoDB; POG091H05FK; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR022462; EpmB.
DR   InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30538; PTHR30538; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF004911; DUF160; 1.
DR   SFLD; SFLDF00314; L-lysine_2_3-aminomutase_(yjeK; 1.
DR   SFLD; SFLDG01070; PLP-dependent; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   TIGRFAMs; TIGR03821; EFP_modif_epmB; 1.
DR   TIGRFAMs; TIGR00238; TIGR00238; 1.
PE   4: Predicted;
DR   PRODOM; C5BDL1.
DR   SWISS-2DPAGE; C5BDL1.
KW   4Fe-4S {ECO:0000256|PIRSR:PIRSR004911-1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Iron {ECO:0000256|PIRSR:PIRSR004911-1};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR004911-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004911-1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603739-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN      120    263       Radical_SAM. {ECO:0000259|Pfam:PF04055}.
FT   METAL       120    120       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR004911-1}.
FT   METAL       124    124       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR004911-1}.
FT   METAL       127    127       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|PIRSR:PIRSR004911-1}.
FT   MOD_RES     332    332       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR603739-50}.
SQ   SEQUENCE   342 AA;  38687 MW;  CB4F7E7E4A4B3873 CRC64;
     MAHIITQKGQ PREDWLQQLA DVVTDPADLL AQLGLSDHPQ WLAGCEARRL FPLRVPHAFI
     SRIRRGDPND PLLRQVMSDA AEFIETPGFS TDPLAEQHSV VPGLLHKYQN RALLLVKGSC
     AVNCRYCFRR HFPYQENQGT RANWQRAVAY LCEHPELDEI IFSGGDPLMA KDHELDWLFT
     QLEQLPHLRR LRIHSRLPVV IPARVTDALC QRMADSRLQM ILVTHINHAN EIDEALSEAM
     ERLKQAGVTL LNQSVLLRGI NDNADTLAAL SNALFEAGIL PYYLHVLDKV QGGAHFMVPD
     DEARRLMNGL LSRVSGYLVP RLTREIGGEP SKTPLDLHLR QQ
//

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