ID A0A2U2J7I4_9FLAO Unreviewed; 322 AA.
AC A0A2U2J7I4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=D-arabinose 5-phosphate isomerase {ECO:0000313|EMBL:PWG04300.1};
GN ORFNames=DIS07_12890 {ECO:0000313|EMBL:PWG04300.1};
OS Polaribacter aquimarinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2100726 {ECO:0000313|EMBL:PWG04300.1, ECO:0000313|Proteomes:UP000245670};
RN [1] {ECO:0000313|EMBL:PWG04300.1, ECO:0000313|Proteomes:UP000245670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZY113 {ECO:0000313|EMBL:PWG04300.1,
RC ECO:0000313|Proteomes:UP000245670};
RA Lu D.;
RT "Polaribacter aquimarinus sp. nov., isolated from sediment in a sediment of
RT sea.";
RL Submitted (MAY-2018) 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:PWG04300.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QFFG01000006; PWG04300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2J7I4; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000245670; 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:PWG04300.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000245670};
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 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; 34799 MW; 09C9833FD997A8E2 CRC64;
MKKTNSIIKT AKKTILIESN AIANLANLID ADFEKAVNFI LNSKGRVILT GIGKSANIGA
KIVATFNSTG TPAIFMHAAD AIHGDLGNVQ TDDVVICISK SGNTPEIKVL VPLIKNYGNK
IVAITGNVDS YLGEHADFTI NAYVEQEACP NNLAPTTSTT AQLVLGDALA VCLLELKGFT
SKDFAKYHPG GALGKKLYLR VSDLIKNNQI PKVNESDSIA KVIIEISEKR LGVTAVMNKE
KLVGIITDGD IRRMLSKTTQ ISKFTAKDIM GNNPKTIHKN AMAIDALQIM EKNSITQMLV
INNKNKYVGV VHLHDLIKEG IF
//