ID A0A1Y5ENQ7_9GAMM Unreviewed; 327 AA.
AC A0A1Y5ENQ7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=A9Q82_01180 {ECO:0000313|EMBL:OUR84090.1};
OS Cycloclasticus sp. 46_120_T64.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=1856281 {ECO:0000313|EMBL:OUR84090.1, ECO:0000313|Proteomes:UP000195872};
RN [1] {ECO:0000313|Proteomes:UP000195872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hu P., Dubinsky E.A., Probst A.J., Wang J., Sieber C.M.K., Tom L.M.,
RA Gardinali P., Banfield J.F., Atlas R.M., Andersen G.L.;
RT "Simulation of Deepwater Horizon oil plume reveals substrate specialization
RT within a complex community of hydrocarbon-degraders.";
RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2017).
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:OUR84090.1}.
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DR EMBL; MAAM01000002; OUR84090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5ENQ7; -.
DR Proteomes; UP000195872; 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:0000256|PIRNR:PIRNR004692, ECO:0000313|EMBL:OUR84090.1};
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..267
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; 34387 MW; DE5919F7629A8954 CRC64;
MPINNQQRDK LKQLGMAVVN TEAEAIAGLR HHINDNFAHA CQLMLACEGK VVVIGMGKSG
HIGSKIAATL ASTGTPAFFI HPGEASHGDL GMITKNDVAI ALSNSGETGE VLSILPIIKR
LGVPLISISG NPTSTLATLS DAAIDASIEK EACPLGLAPT SSTTAALVMG DALAIALLEA
RGFTEKDFAL SHPGGSLGRR LLLHVSDIMH QGDDIPIIEQ QQLVSAALLE MTEKKLGMTA
IVNSTDELVG IFTDGDLRRM LENNTDIHNT EIRQVMTAGG STIGSGRLAV EALQLMQDKQ
INALLVIDNK KLVGALNMHD MLKAGLS
//
