ID A0A0Q4BZ60_9SPHN Unreviewed; 328 AA.
AC A0A0Q4BZ60;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=D-arabinose 5-phosphate {ECO:0000313|EMBL:KQM18272.1};
GN ORFNames=ASE49_08585 {ECO:0000313|EMBL:KQM18272.1};
OS Novosphingobium sp. Leaf2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM18272.1, ECO:0000313|Proteomes:UP000050893};
RN [1] {ECO:0000313|EMBL:KQM18272.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM18272.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM18272.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM18272.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000256|ARBA:ARBA00008165, ECO:0000256|PIRNR:PIRNR004692}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQM18272.1}.
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DR EMBL; LMJY01000017; KQM18272.1; -; Genomic_DNA.
DR RefSeq; WP_056772664.1; NZ_LMJY01000017.1.
DR AlphaFoldDB; A0A0Q4BZ60; -.
DR STRING; 1735670.ASE49_08585; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000050893; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; 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 Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000050893};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 44..187
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 212..272
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 277..328
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 62
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 114
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 155
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 196
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 328 AA; 34905 MW; 2137EB4379CB7DFB CRC64;
MKTVFLQRRH SASALKTLDI ELEALQALKT ALKGPEMRDA VDRAIQTLAA TRGRVIVTGM
GKSGHIARKI AATMRSTGTS ALYLHPGEAS HGDLGVITKD DVVLAITWSG ETSELNDIFY
YCNRFGVKLI VATSHPESTA GRAADICLSM PPVREACPNE LAPTSSTTVQ LVLGDALAVA
LIEARGFSPS DFHVFHPGGK LGAQLARVGQ VMGTGDAVPR VSRDASLTSA TLEMSRKRYG
CTAVVDDDDK LVGAFTDGDL RRCIAVHDLN DNIGLHMSPR PVTVEADMLV SEALAILNEN
AVSVLFVVDG EKLVGIVHMH DLVRASVA
//
