(data stored in ACNUC7421 zone)

SWISSPROT: C5B733_EDWI9

ID   C5B733_EDWI9            Unreviewed;       328 AA.
AC   C5B733;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 53.
DE   RecName: Full=Arabinose 5-phosphate isomerase {ECO:0000256|PIRNR:PIRNR004692};
DE            Short=API {ECO:0000256|PIRNR:PIRNR004692};
DE            EC=5.3.1.13 {ECO:0000256|PIRNR:PIRNR004692};
GN   OrderedLocusNames=NT01EI_0578 {ECO:0000313|EMBL:ACR67807.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67807.1, 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   -!- CATALYTIC ACTIVITY: D-arabinose 5-phosphate = D-ribulose 5-
CC       phosphate. {ECO:0000256|PIRNR:PIRNR004692}.
CC   -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC       {ECO:0000256|PIRNR:PIRNR004692}.
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DR   EMBL; CP001600; ACR67807.1; -; Genomic_DNA.
DR   RefSeq; WP_015870006.1; NC_012779.2.
DR   ProteinModelPortal; C5B733; -.
DR   STRING; 634503.NT01EI_0578; -.
DR   EnsemblBacteria; ACR67807; ACR67807; NT01EI_0578.
DR   GeneID; 7960346; -.
DR   KEGG; eic:NT01EI_0578; -.
DR   PATRIC; fig|634503.3.peg.523; -.
DR   eggNOG; ENOG4105C2X; Bacteria.
DR   eggNOG; COG0517; LUCA.
DR   eggNOG; COG0794; LUCA.
DR   HOGENOM; HOG000264729; -.
DR   KO; K06041; -.
DR   OMA; FMHAADA; -.
DR   OrthoDB; POG091H01V1; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05014; SIS_Kpsf; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR004800; KdsD/KpsF-type.
DR   InterPro; IPR001347; SIS.
DR   InterPro; IPR035474; SIS_Kpsf.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF01380; SIS; 1.
DR   PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR   TIGRFAMs; TIGR00393; kpsF; 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B733.
DR   SWISS-2DPAGE; C5B733.
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR004692,
KW   ECO:0000313|EMBL:ACR67807.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT   DOMAIN       41    184       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   DOMAIN      210    268       CBS. {ECO:0000259|PROSITE:PS51371}.
FT   DOMAIN      277    328       CBS. {ECO:0000259|PROSITE:PS51371}.
FT   METAL        82     82       Zinc. {ECO:0000256|PIRSR:PIRSR004692-2}.
FT   BINDING      82     82       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR004692-1}.
FT   BINDING      88     88       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR004692-1}.
FT   BINDING     222    222       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR004692-1}.
FT   BINDING     275    275       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR004692-1}.
FT   SITE         59     59       Catalytically relevant.
FT                                {ECO:0000256|PIRSR:PIRSR004692-3}.
FT   SITE        111    111       Catalytically relevant.
FT                                {ECO:0000256|PIRSR:PIRSR004692-3}.
FT   SITE        152    152       Catalytically relevant.
FT                                {ECO:0000256|PIRSR:PIRSR004692-3}.
FT   SITE        193    193       Catalytically relevant.
FT                                {ECO:0000256|PIRSR:PIRSR004692-3}.
SQ   SEQUENCE   328 AA;  35300 MW;  C74259D4FD766066 CRC64;
     MSHMELQPDF DFQQAGKDVL RIEREGLAHL DLFINQDFSR ACDAMLRCRG KVVVMGMGKS
     GHIGRKIAAT LASTGTSAFF VHPGEASHGD LGMVEQRDVV LAISNSGESQ EIQALIPVLK
     RQNVTLICMT NNPDSAMGRA ADIHLCIRVP QEACPMGLAP TTSTTATLVM GDALAVALLQ
     ARGFTAEDFA LSHPGGALGR KLLLRVSDIM HSGDEVPMVS PTASLRDALL EITRKNLGLT
     VICGPDAHID GIFTDGDLRR IFDMGINLNN AKIADVMTRG GIRIRPTALA VDALNLMQER
     HITSLLVAEN DRLIGVVHMH DMLRAGVV
//

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