ID A0A0P1EPQ8_9RHOB Unreviewed; 320 AA.
AC A0A0P1EPQ8;
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=Arabinose 5-phosphate isomerase KdsD {ECO:0000313|EMBL:CUH52137.1};
DE EC=5.3.1.13 {ECO:0000313|EMBL:CUH52137.1};
GN Name=kdsD_2 {ECO:0000313|EMBL:CUH52137.1};
GN ORFNames=SHM7688_01577 {ECO:0000313|EMBL:CUH52137.1};
OS Shimia marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH52137.1, ECO:0000313|Proteomes:UP000054823};
RN [1] {ECO:0000313|EMBL:CUH52137.1, ECO:0000313|Proteomes:UP000054823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH52137.1,
RC ECO:0000313|Proteomes:UP000054823};
RG Swine Surveillance;
RL Submitted (SEP-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}.
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DR EMBL; CYPW01000013; CUH52137.1; -; Genomic_DNA.
DR RefSeq; WP_058239364.1; NZ_FOMU01000013.1.
DR AlphaFoldDB; A0A0P1EPQ8; -.
DR STRING; 321267.SHM7688_01577; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000054823; Unassembled WGS sequence.
DR GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0097367; F:carbohydrate derivative binding; 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 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:CUH52137.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000054823};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 41..184
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 209..266
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
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 320 AA; 34060 MW; 7724819E869EABA5 CRC64;
MKYDKRLHEK SLSQITNDVL RKEGNALLHF ATTQDDAIVE AIDLILRNAG PVIVSGVGKS
GHIGQKIAAT LRSLGKPAAF LHASEASHGD LGIIQKDSTV MILSNSGETT ELSDLMLYCR
AYNLPVISMT SNCESTLANF SDVTICYGKT QEACMNGLAP TTSTTLCLAI GDAIAVGVSF
RLGIAPEDFR RWHPGGKLGA RISLVSDVMR KGADMPLVNP DATIMESLLV MAEKSVGSVI
ICEGNDVLGI ATDGDVRRNF EKPATSHIRE IATASPVYIS KDLTATEAAE HMSQRGITSC
IVGTSGANVE GYLHIHDCIS
//