ID L0EST3_LIBCB Unreviewed; 323 AA.
AC L0EST3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Arabinose 5-phosphate isomerase {ECO:0000313|EMBL:AGA64569.1};
DE EC=5.3.1.13 {ECO:0000313|EMBL:AGA64569.1};
GN OrderedLocusNames=B488_05770 {ECO:0000313|EMBL:AGA64569.1};
OS Liberibacter crescens (strain BT-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=1215343 {ECO:0000313|EMBL:AGA64569.1, ECO:0000313|Proteomes:UP000010799};
RN [1] {ECO:0000313|EMBL:AGA64569.1, ECO:0000313|Proteomes:UP000010799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-1 {ECO:0000313|EMBL:AGA64569.1,
RC ECO:0000313|Proteomes:UP000010799};
RX PubMed=23408754; DOI=10.4056/sigs.3326772;
RA Leonard M.T., Fagen J.R., Davis-Richardson A.G., Davis M.J., Triplett E.W.;
RT "Complete genome sequence of Liberibacter crescens BT-1.";
RL Stand. Genomic Sci. 7:271-283(2012).
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; CP003789; AGA64569.1; -; Genomic_DNA.
DR RefSeq; WP_015272996.1; NC_019907.1.
DR AlphaFoldDB; L0EST3; -.
DR STRING; 1215343.B488_05770; -.
DR KEGG; lcc:B488_05770; -.
DR PATRIC; fig|1215343.11.peg.587; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR HOGENOM; CLU_040681_13_1_5; -.
DR Proteomes; UP000010799; 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:AGA64569.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000010799};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 38..181
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 206..265
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 271..323
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 56
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 108
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 149
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 190
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 323 AA; 34756 MW; B0E13A446B592B24 CRC64;
MMTTAVQSAI RSISIERNAL LSLELALSQK LAQPFSKAVE IISKISGRVI VTGVGKSGHI
GAKLAATLAS TGTPAFFVHA AEANHGDLGM IAQDDVIIAM SWSGETDELK AILCYSKRFS
IPLIAITSGE KSTLAAHADI LLILPKEQEA CPHGLAPTTS TMMQLAIGDA LAVALLEAHN
FSADDFRVFH PGGKLGSLLR RVVDVMHSGE RIPLVPLGTK LSEAIQILSE KKFGCVAIIN
NHRQLVGIMT EGDVFRNFEK DLTKLIVDDL MSKDPKTVMV DTLATIAMSL LQKYNISVLI
VVDPHRRPVG ILHFLDLLRV GIV
//
