ID M1LA02_9PROT Unreviewed; 328 AA.
AC M1LA02;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 44.
DE SubName: Full=Arabinose-5-phosphate isomerase {ECO:0000313|EMBL:AGF49348.1};
DE EC=5.3.1.13 {ECO:0000313|EMBL:AGF49348.1};
GN ORFNames=ST1E_0087 {ECO:0000313|EMBL:AGF49348.1};
OS Candidatus Kinetoplastibacterium galatii TCC219.
OC Bacteria; Pseudomonadota; Betaproteobacteria;
OC Candidatus Kinetoplastibacterium.
OX NCBI_TaxID=1208921 {ECO:0000313|EMBL:AGF49348.1, ECO:0000313|Proteomes:UP000011658};
RN [1] {ECO:0000313|EMBL:AGF49348.1, ECO:0000313|Proteomes:UP000011658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC219 {ECO:0000313|EMBL:AGF49348.1,
RC ECO:0000313|Proteomes:UP000011658};
RX PubMed=23345457;
RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA Teixeira M.M., Camargo E.P., Buck G.A.;
RT "Genome evolution and phylogenomic analysis of candidatus
RT kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT and angomonas.";
RL Genome Biol. Evol. 5:338-350(2013).
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; CP003806; AGF49348.1; -; Genomic_DNA.
DR RefSeq; WP_015389832.1; NC_020284.1.
DR AlphaFoldDB; M1LA02; -.
DR STRING; 1208921.ST1E_0087; -.
DR KEGG; kga:ST1E_0087; -.
DR PATRIC; fig|1208921.3.peg.639; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR HOGENOM; CLU_040681_13_1_4; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000011658; 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:AGF49348.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 39..182
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 208..267
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 276..328
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 57
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 109
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 150
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 191
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 328 AA; 35149 MW; F9D7A65B9D6A23D4 CRC64;
MDIKISNEDV ISSAHRTLRI EARAIEEISF RLNNEFILSV KMLLSCKGRV IVSGIGKTGH
IGRKIAATLA STGTPAFFVH AAEAMHGDLG MLTKNDVLVA ISYSGSGPEL LSILPTAKRL
GIKIIAITGN IKSEIANLSD SILDINVQQE ACPLNLAPTA STTAALALGD ALAVACLELR
CFNLNDFARS HPGGTLGRNL LTLVQDIMRP IELLPIVHPS LSILEALDII SSKNMGMAII
IDDNKIPLGI FTDGDLRRLL IKHKGDICKI SILSGMSSKP YCIPPRALAI EAAKTMHEKQ
INQIIVLDEG SSLIGALHIH DLINAKII
//