ID A0A0F3LGS4_9CAUL Unreviewed; 330 AA.
AC A0A0F3LGS4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=D-arabinose 5-phosphate {ECO:0000313|EMBL:KJV42780.1};
GN ORFNames=VH88_02850 {ECO:0000313|EMBL:KJV42780.1};
OS Brevundimonas sp. KM4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1628191 {ECO:0000313|EMBL:KJV42780.1, ECO:0000313|Proteomes:UP000033583};
RN [1] {ECO:0000313|EMBL:KJV42780.1, ECO:0000313|Proteomes:UP000033583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM4 {ECO:0000313|EMBL:KJV42780.1,
RC ECO:0000313|Proteomes:UP000033583};
RA Sulaiman J., Priya K., Chan K.-G.;
RT "Draft genome sequence of Brevundimonas sp. KM4.";
RL Submitted (MAR-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:KJV42780.1}.
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; JZRG01000006; KJV42780.1; -; Genomic_DNA.
DR RefSeq; WP_045809919.1; NZ_JZRG01000006.1.
DR AlphaFoldDB; A0A0F3LGS4; -.
DR PATRIC; fig|1628191.3.peg.2334; -.
DR Proteomes; UP000033583; 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 Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 44..187
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 212..273
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 278..330
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 330 AA; 34697 MW; 48E71E28E6FD46D4 CRC64;
MTEIAHSTPD DIAVMTDRAR EVVRLNIEAL EALERSIDVS LARAVDVIMS RPGYVVVTGM
GKSGHIGGKI AATLASTGTN AFFVHPAEMS HGDLGMLRPD VTVLAISNSG ESRELRDPLI
YCQRNGIPVI AITQRPASFL GRNAAVCLTM PKVAEACPNG LAPTTSTLMT LALGDALAMV
LMDRREFTAM DFGLHHPGGA LGMSLQSVRE WMGDNAAVPA SVPLNASFGD VVSAITEGRK
GAVAVLDADG ALAGIVTDGD LRRAFQRDTT HLTAADIMSA NPITVDPDAR MSDVVDLLTA
NKIANLFVVE DGKPTAIVHI AELMQAGYVA
//
