ID A0A191ZE60_9GAMM Unreviewed; 323 AA.
AC A0A191ZE60;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=A9404_01135 {ECO:0000313|EMBL:ANJ66161.1};
OS Halothiobacillus diazotrophicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Halothiobacillaceae; Halothiobacillus.
OX NCBI_TaxID=1860122 {ECO:0000313|EMBL:ANJ66161.1, ECO:0000313|Proteomes:UP000078596};
RN [1] {ECO:0000313|EMBL:ANJ66161.1, ECO:0000313|Proteomes:UP000078596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS2 {ECO:0000313|EMBL:ANJ66161.1,
RC ECO:0000313|Proteomes:UP000078596};
RA Luo J., Tan X., Lin W.;
RT "Insight into the functional genes involving in sulfur oxidation in Pearl
RT River water.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; CP016027; ANJ66161.1; -; Genomic_DNA.
DR RefSeq; WP_066097893.1; NZ_CP016027.1.
DR AlphaFoldDB; A0A191ZE60; -.
DR STRING; 1860122.A9404_01135; -.
DR KEGG; haz:A9404_01135; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000078596; Chromosome.
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:ANJ66161.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000078596};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 35..178
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 204..263
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; 34347 MW; 5A54DA557FB9049A CRC64;
MNPNNLLAMA KQVIDIETQA CLALSERIDE AFVNACELML RCEGRVIVTG MGKSGHIGGK
IAATLASTGT PAFFVHPGEA SHGDLGMITR KDVVLALSNS GETAEVLAIL PVIKRLGSPL
IAMTGKPQST LAQAADAHLN TSVAREACPL NLAPTASTTA ALVMGDALAV ALLDARAFQP
EDFALSHPGG ALGRRLLLRV RDVMHTGERI PKVQYNQTIK QTLITISSGG LGMAAVIDDD
EKLLGLFTDG DLRRILDQTE FDLNLPIEKV MTRNPRTCSE DILAAEAMAI MERDKINGLL
VLDDNRTVIG ALNMHDLLRA GVA
//
