ID A0A011QQC7_9PROT Unreviewed; 327 AA.
AC A0A011QQC7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE SubName: Full=Arabinose 5-phosphate isomerase KdsD {ECO:0000313|EMBL:EXI91462.1};
DE EC=5.3.1.13 {ECO:0000313|EMBL:EXI91462.1};
GN Name=kdsD {ECO:0000313|EMBL:EXI91462.1};
GN ORFNames=AW12_01290 {ECO:0000313|EMBL:EXI91462.1};
OS Candidatus Accumulibacter sp. BA-94.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454005 {ECO:0000313|EMBL:EXI91462.1, ECO:0000313|Proteomes:UP000020878};
RN [1] {ECO:0000313|EMBL:EXI91462.1, ECO:0000313|Proteomes:UP000020878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-94 {ECO:0000313|Proteomes:UP000020878};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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:EXI91462.1}.
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DR EMBL; JEMZ01000064; EXI91462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011QQC7; -.
DR STRING; 1454005.AW12_01290; -.
DR PATRIC; fig|1454005.3.peg.1253; -.
DR Proteomes; UP000020878; 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 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:EXI91462.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000020878};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 39..182
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 208..266
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 275..327
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 57
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 109
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 150
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 191
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 327 AA; 34389 MW; 8C2C38A68B931183 CRC64;
MSQTRPSANA LDLARQVMRI EADAVLALAS RIGDEFLQAL LLILNCPGRI IVSGMGKSGH
VGRKIASTFA STGTPAYFVH PAEASHGDLG MITRDDVLIA LSNSGESAEL LTIVPIIKRQ
GARLISMTGN PQSSLAVEAD VHLDAAVAQE ACPLNLAPTA STTAALALGD ALAVALLDSR
GFGAEDFARS HPGGSLGRRL LTHVRDVMHS GPALPEVLPA TSLHDAILEI TRGGIGMTAV
VDPQRRVIGI VTDGDLRRAF ARSLDLRTLV AADIMGRSPR SIAPDRLAVE AVAMMEEHKI
NQLPVVDRGG ILVGALNMHD LFRAKVI
//
