ID A0A0F2P3H2_9GAMM Unreviewed; 323 AA.
AC A0A0F2P3H2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 13-SEP-2023, entry version 27.
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=VR73_07455 {ECO:0000313|EMBL:KJS07955.1};
OS Gammaproteobacteria bacterium BRH_c0.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1629722 {ECO:0000313|EMBL:KJS07955.1, ECO:0000313|Proteomes:UP000033581};
RN [1] {ECO:0000313|EMBL:KJS07955.1, ECO:0000313|Proteomes:UP000033581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c0 {ECO:0000313|EMBL:KJS07955.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KJS07955.1}.
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DR EMBL; LADM01000056; KJS07955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2P3H2; -.
DR STRING; 1629722.VR73_07455; -.
DR PATRIC; fig|1629722.3.peg.2528; -.
DR Proteomes; UP000033581; 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:KJS07955.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 35..178
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 204..262
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 271..323
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 53
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 105
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 146
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 187
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 323 AA; 33969 MW; 5D226612A660BD4D CRC64;
MTDANFIASA KRTVQLEAEA VHNLEARIGT DFARACELIL ACKGRTIVTG MGKSGHVGRK
IAATLASTGS PAFFVHPGEA SHGDLGMITA SDVVIAISSS GSTAEVVTLL PLIKRLGIPL
ISMTGNPSSP LARFADALLD IAVSKEACPL DLAPTTSTTV TLVMGDALAI ALLEARGFTA
DDFALSHPGG ALGRKLLLRV EDIMHGGDQV PRVQEASLLR DTLLEMTEKG FGMTTVVSTE
DELLGVFTDG DLRRAVDQGI DINSVTIGQV MTRNCQTISA DILAAEALRI METRKITALV
VEDGSRHPVG VIHMHDILRA GII
//
