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Entry: I0QZF1_9GAMM
LinkDB: I0QZF1_9GAMM
Original site: I0QZF1_9GAMM 
ID   I0QZF1_9GAMM            Unreviewed;       327 AA.
AC   I0QZF1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Arabinose 5-phosphate isomerase {ECO:0000256|PIRNR:PIRNR004692};
DE            Short=API {ECO:0000256|PIRNR:PIRNR004692};
DE            EC=5.3.1.13 {ECO:0000256|PIRNR:PIRNR004692};
GN   ORFNames=SPM24T3_01295 {ECO:0000313|EMBL:EIC86674.1};
OS   Serratia sp. M24T3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC86674.1, ECO:0000313|Proteomes:UP000011072};
RN   [1] {ECO:0000313|EMBL:EIC86674.1, ECO:0000313|Proteomes:UP000011072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M24T3 {ECO:0000313|EMBL:EIC86674.1,
RC   ECO:0000313|Proteomes:UP000011072};
RX   PubMed=22740681; DOI=10.1128/JB.00670-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Serratia sp. Strain M24T3, Isolated from Pinewood
RT   Disease Nematode Bursaphelenchus xylophilus.";
RL   J. Bacteriol. 194:3764-3764(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-arabinose 5-phosphate = D-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:23104, ChEBI:CHEBI:57693, ChEBI:CHEBI:58121;
CC         EC=5.3.1.13; Evidence={ECO:0000256|PIRNR:PIRNR004692};
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:EIC86674.1}.
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DR   EMBL; AJHJ01000001; EIC86674.1; -; Genomic_DNA.
DR   RefSeq; WP_009634873.1; NZ_AJHJ01000001.1.
DR   AlphaFoldDB; I0QZF1; -.
DR   STRING; 932213.SPM24T3_01295; -.
DR   PATRIC; fig|932213.3.peg.273; -.
DR   eggNOG; COG0517; Bacteria.
DR   eggNOG; COG0794; Bacteria.
DR   OrthoDB; 9762536at2; -.
DR   Proteomes; UP000011072; 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; 2.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR004692, ECO:0000313|EMBL:EIC86674.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT   DOMAIN          40..183
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          209..269
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          276..327
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT   SITE            58
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            110
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            151
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            192
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ   SEQUENCE   327 AA;  35349 MW;  6A655D16215E3A61 CRC64;
     MTTFDNEKFN FVQVGKQVLL TEREGLEQLD QYINDDFTRA CEMMFQCSGK IIVMGMGKSG
     HVARKMAATF ASTGTPAFFV HPAEASHGDL GMVSTQDIVI LISNSGESHE ILALIPVLKR
     LDIRLICLTA NPESSMGKAA DVHICVKVPK EACPLGLAPT TSTTAVMVMG DALAVALLEA
     RGFTAEDFAL SHPGGALGRK LLLRVSDIMH TGSEIPQVSR DASLRDALLE ITRKNLGMTV
     ITDDLMKIEG IFTDGDLRRI FDMGVNVNEA KITDVMTPGG IRVRPVLLAV DALNLMQEKN
     ITCVMVADGD RLLGVVHMHD MLRAGVV
//
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