ID A0A0L6T544_9BURK Unreviewed; 333 AA.
AC A0A0L6T544;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Arabinose 5-phosphate isomerase {ECO:0000313|EMBL:KNZ31261.1};
GN ORFNames=AD742_18970 {ECO:0000313|EMBL:KNZ31261.1};
OS Methylibium sp. NZG.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1686064 {ECO:0000313|EMBL:KNZ31261.1, ECO:0000313|Proteomes:UP000053102};
RN [1] {ECO:0000313|Proteomes:UP000053102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bi G.;
RT "Draft Genome Sequences of the MTBE Degrading Bacterium Methylibium sp.
RT NZG.";
RL Submitted (JUL-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:KNZ31261.1}.
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DR EMBL; LGRD01000032; KNZ31261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6T544; -.
DR STRING; 1686064.AD742_18970; -.
DR PATRIC; fig|1686064.3.peg.3690; -.
DR Proteomes; UP000053102; 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:KNZ31261.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000053102};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 39..182
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 208..267
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 281..333
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 333 AA; 34964 MW; 3A107F31568E9F70 CRC64;
MPTAFDDARA LRLACKTFDI EAQALLGLKA RLGPSFARTV QAMLNCRGRV VVMGMGKSGH
VGRKIAATLA STGTPAMFVH PAEASHGDLG MVTPGDIVLA ISNSGESDEL AAIVPAIKRL
GTVLVAITGR TDSSLAQHAD LVLSSAVDQE ACPLNLAPTA STAAQMAMGD ALAVALLDAR
GFREEDFARS HPGGSLGRKL LIHVRDLMRS GDALPRVGPD ATFNEMLREM TGKGLGFTAI
SEADSGQVLG IFTDGDLRRL IERGAGERGA DLRSLHARDV MHPAPRRVRD DALAVEAAEV
MEQHRVTSVL VVDATGVLVG ALNTNDLLRA KVI
//
