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Database: UniProt
Entry: A0A1B9XY03_9FLAO
LinkDB: A0A1B9XY03_9FLAO
Original site: A0A1B9XY03_9FLAO 
ID   A0A1B9XY03_9FLAO        Unreviewed;       322 AA.
AC   A0A1B9XY03;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=D-arabinose 5-phosphate isomerase {ECO:0000313|EMBL:OCK42311.1};
GN   ORFNames=BA195_11860 {ECO:0000313|EMBL:OCK42311.1};
OS   Tenacibaculum soleae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=447689 {ECO:0000313|EMBL:OCK42311.1, ECO:0000313|Proteomes:UP000093186};
RN   [1] {ECO:0000313|EMBL:OCK42311.1, ECO:0000313|Proteomes:UP000093186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-KL19 {ECO:0000313|EMBL:OCK42311.1,
RC   ECO:0000313|Proteomes:UP000093186};
RA   Eisen J.A., Coil D.A., Lujan K.M.;
RT   "Draft Genome Sequence of Tenacibaculum soleae UCD-KL19.";
RL   Submitted (JUN-2016) 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:OCK42311.1}.
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DR   EMBL; MAKX01000024; OCK42311.1; -; Genomic_DNA.
DR   RefSeq; WP_068705827.1; NZ_MAKX01000024.1.
DR   AlphaFoldDB; A0A1B9XY03; -.
DR   STRING; 447689.BA195_11860; -.
DR   OrthoDB; 9762536at2; -.
DR   Proteomes; UP000093186; Unassembled WGS sequence.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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:OCK42311.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093186};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT   DOMAIN          36..179
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          204..261
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          270..322
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-1"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-1"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-1"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-1"
FT   SITE            54
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            106
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            147
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            188
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ   SEQUENCE   322 AA;  34502 MW;  C1817DE874C11B71 CRC64;
     MKDANAILST AKETILLESN AIANLANLLN SSFVEAVNFI FNSKGRVIVT GIGKSANIAN
     KMVATFNSTG TPAVFMHAAD AIHGDLGNVQ NNDTVICISK SGNTPEIKVL VPLIKSSKNK
     IIAITGNPDS FLGKNADFLL NSFVEKEACP NNLAPTTSTT AQLVLGDALA VCLLDLRGFT
     SSDFAKYHPG GALGKRLYLR VADLIKNNQL PKVNSTDKVT QVIVEISEKR LGVTAVVEDS
     KIVGIITDGD IRRMLSKTTK IDKLTANDIM SKNPKTIHVE AMAVEALDTL ENSSITQILV
     TDNDNNYVGV VHLHDLIKEG IF
//
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