ID A0A0A1YF07_9PSED Unreviewed; 324 AA.
AC A0A0A1YF07;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=TMS3_0119505 {ECO:0000313|EMBL:KFX68430.1};
OS Pseudomonas taeanensis MS-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX68430.1, ECO:0000313|Proteomes:UP000030063};
RN [1] {ECO:0000313|EMBL:KFX68430.1, ECO:0000313|Proteomes:UP000030063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-3 {ECO:0000313|EMBL:KFX68430.1,
RC ECO:0000313|Proteomes:UP000030063};
RX PubMed=24407626;
RA Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA Choi J.S., Kahng H.Y., Kim S.I.;
RT "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT Seashore.";
RL Genome Announc. 2:0-0(2014).
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:KFX68430.1}.
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DR EMBL; AWSQ01000006; KFX68430.1; -; Genomic_DNA.
DR RefSeq; WP_025166881.1; NZ_AWSQ01000006.1.
DR AlphaFoldDB; A0A0A1YF07; -.
DR STRING; 1395571.TMS3_0119505; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000030063; 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:KFX68430.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000030063};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 36..179
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 205..263
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 272..324
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 54
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 106
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 147
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 188
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 324 AA; 34545 MW; A064B7B9318B2FE9 CRC64;
MSQSHELIKS AHRTIRLEIE AVEELLQRID TDFIRACELI LASKGRVVVV GMGKSGHIGN
KIAATLASTG TTAFFVHPAE ASHGDMGMIT RDDVVLALSN SGSTAEIVTL LPLIKRLGIT
LISMTGNPDS PLAKAAEVNL DARVSQEACP LNLAPTSSTT ASLVLGDALA IALLEARGFT
AEDFAFSHPG GALGRRLLLK VENVMHAGKS LPQVQRGTSL REALLEMTQK GLGMTVVLEQ
DGRLAGIFTD GDLRRTLDRG IDVRHATIDE VMTIHGKTAR AEMLAAEALK IMEDHKISGL
VVVDDDDRPV GALNMHDLLR AGVM
//
