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Database: UniProt
Entry: A0A1I2P5C9_9BACT
LinkDB: A0A1I2P5C9_9BACT
Original site: A0A1I2P5C9_9BACT 
ID   A0A1I2P5C9_9BACT        Unreviewed;       324 AA.
AC   A0A1I2P5C9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Arabinose-5-phosphate isomerase {ECO:0000313|EMBL:SFG08681.1};
GN   ORFNames=SAMN05216383_1055 {ECO:0000313|EMBL:SFG08681.1};
OS   Prevotella sp. KH2C16.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1855325 {ECO:0000313|EMBL:SFG08681.1, ECO:0000313|Proteomes:UP000198560};
RN   [1] {ECO:0000313|Proteomes:UP000198560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH2C16 {ECO:0000313|Proteomes:UP000198560};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOOW01000005; SFG08681.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2P5C9; -.
DR   STRING; 1855325.SAMN05216383_1055; -.
DR   OrthoDB; 9762536at2; -.
DR   Proteomes; UP000198560; 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: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; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51371; CBS; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Isomerase {ECO:0000313|EMBL:SFG08681.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198560}.
FT   DOMAIN          41..184
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          276..324
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   SITE            59
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            111
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            152
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            193
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ   SEQUENCE   324 AA;  35591 MW;  5FA3EF15F672EC1B CRC64;
     MTEKATERLN HAREFAIQAL RDESDALLEL IPQLDENFDH AVRMMFECKG KIIVTGVGKS
     GNIGAKIAAT LASTGTPAFF INPLDVYHGD LGVMTSEDVV LALSNSGQTD ELLRFIPMVL
     HMNVPIIAMT GNENSLLAKY SNAHIKVWVK KEACPLNLAP TSSTTAALAM GDALAIALME
     ARDFKPKDFA QFHPGGELGK RLLTTAEDVM RSDELPIIPK EMHLGEAIIH VSKGKLGLGV
     SLENGKVIGL ITDGDIRRAM EKWQARFFDR TVSDIMTTNP KTVLPTTKIT DIQQIMNRHK
     IHTVLVVDKE DHLLGVVDHY SCMI
//
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