ID A0A0A1F7F3_9BURK Unreviewed; 331 AA.
AC A0A0A1F7F3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Arabinose 5-phosphate isomerase {ECO:0000313|EMBL:AIY39619.1};
DE EC=5.3.1.13 {ECO:0000313|EMBL:AIY39619.1};
GN ORFNames=LT85_0459 {ECO:0000313|EMBL:AIY39619.1};
OS Collimonas arenae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=279058 {ECO:0000313|EMBL:AIY39619.1, ECO:0000313|Proteomes:UP000030302};
RN [1] {ECO:0000313|EMBL:AIY39619.1, ECO:0000313|Proteomes:UP000030302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cal35 {ECO:0000313|EMBL:AIY39619.1,
RC ECO:0000313|Proteomes:UP000030302};
RA Uroz S., Tech J.J., Sawaya N.A., Frey-Klett P., Leveau J.H.J.;
RT "Structure and function of bacterial communities in ageing soils: insights
RT from the Mendocino ecological staircase.";
RL Soil Biol. Biochem. 69:265-274(2014).
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000256|ARBA:ARBA00008165, ECO:0000256|PIRNR:PIRNR004692}.
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DR EMBL; CP009962; AIY39619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1F7F3; -.
DR STRING; 279058.LT85_0459; -.
DR KEGG; care:LT85_0459; -.
DR HOGENOM; CLU_040681_13_1_4; -.
DR Proteomes; UP000030302; 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; cd04604; CBS_pair_SIS_assoc; 1.
DR CDD; cd05014; SIS_Kpsf; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR004800; KdsD/KpsF-type.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035474; SIS_Kpsf.
DR NCBIfam; TIGR00393; kpsF; 1.
DR PANTHER; PTHR42745; -; 1.
DR PANTHER; PTHR42745:SF1; ARABINOSE 5-PHOSPHATE ISOMERASE KDSD; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01380; SIS; 1.
DR PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Isomerase {ECO:0000313|EMBL:AIY39619.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 43..186
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 212..270
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 279..331
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 61
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 113
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 154
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 195
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 331 AA; 34950 MW; 9F6E9B1DC3BC3410 CRC64;
MSVTFDAGRA LELARSTLQI EADAITALKN RISDNPHDPF AKAIGLLLGC SGRVVVSGIG
KSGHIARKIA ATLSSTGTPA LFIHPAEAAH GDLGMVTEHD AFIAISNSGE TAELMAIVPI
IKRMGATLIA MTGKPDSALA QLANVHLDVG VVQEACPLNL APTASTTATL AMGDALAVAL
LDARGFREED FARSHPGGAL GRRLLTHVRD VMRSGEAIPA VTADVSMSVA LFEITRKGIA
MTAVVDENFH AVGVFTDGDL RRLIEQVQDF TKLKIADVMH VPPRTIGPDQ LAVDAVQMME
EFRINQLLVT DADGKLVGAL HIHDLTRAKV I
//
