ID E3BG77_9VIBR Unreviewed; 321 AA.
AC E3BG77;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=VIBC2010_12679 {ECO:0000313|EMBL:EFP97943.1};
OS Vibrio caribbeanicus ATCC BAA-2122.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP97943.1, ECO:0000313|Proteomes:UP000002943};
RN [1] {ECO:0000313|EMBL:EFP97943.1, ECO:0000313|Proteomes:UP000002943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP97943.1,
RC ECO:0000313|Proteomes:UP000002943};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(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:EFP97943.1}.
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DR EMBL; AEIU01000033; EFP97943.1; -; Genomic_DNA.
DR RefSeq; WP_009599946.1; NZ_AEIU01000033.1.
DR AlphaFoldDB; E3BG77; -.
DR STRING; 796620.VIBC2010_12679; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000002943; 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:0000256|PIRNR:PIRNR004692, ECO:0000313|EMBL:EFP97943.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002943};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 33..177
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 203..261
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 270..321
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 52
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 104
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 145
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 186
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 321 AA; 33927 MW; 5AF0DB689E9DB6A1 CRC64;
MFDYRAAANK VLTTEINALK KLEHSFNQNF IDVCNLILAN KAGKVVVMGM GKSGHIGKKI
AATFASTGTP AFFVHPGEAA HGDLGMVSPE DIVITISNSG ESSEILGLFP VLKRLKVKMI
SITGKAQSTM AKLSDYHLLI DASEEACPLG LAPTSSTTAT LVMGDALAVA LLQARGFTAE
DFALSHPGGA LGRKLLLRLT DIMHTGDALP LVPANTLIKD ALIEISQKGL GMVAVVCENE
SLVGIFTDGD LRRILDKRID IHSTAIGEVM TVKPTTANAN MLAAEALNLM QENSISGLII
CEDKKVIGAL NMHDLLKAGV L
//
