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Database: UniProt
Entry: A0A109ULB8_9GAMM
LinkDB: A0A109ULB8_9GAMM
Original site: A0A109ULB8_9GAMM 
ID   A0A109ULB8_9GAMM        Unreviewed;       336 AA.
AC   A0A109ULB8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, 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   Name=kdsD {ECO:0000313|EMBL:AMD00229.1};
GN   ORFNames=LOKO_01156 {ECO:0000313|EMBL:AMD00229.1};
OS   Halomonas chromatireducens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=507626 {ECO:0000313|EMBL:AMD00229.1, ECO:0000313|Proteomes:UP000063387};
RN   [1] {ECO:0000313|EMBL:AMD00229.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD00229.1,
RC   ECO:0000313|Proteomes:UP000063387};
RX   PubMed=26988058;
RA   Sharko F.S., Shapovalova A.A., Tsygankova S.V., Komova A.V.,
RA   Boulygina E.S., Teslyuk A.B., Gotovtsev P.M., Namsaraev Z.B.,
RA   Khijniak T.V., Nedoluzhko A.V., Vasilov R.G.;
RT   "Draft Genome Sequence of 'Halomonas chromatireducens' Strain AGD 8-3, a
RT   Haloalkaliphilic Chromate- and Selenite-Reducing Gammaproteobacterium.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|EMBL:AMD00229.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD00229.1,
RC   ECO:0000313|Proteomes:UP000063387};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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; CP014226; AMD00229.1; -; Genomic_DNA.
DR   RefSeq; WP_066446215.1; NZ_CP014226.1.
DR   AlphaFoldDB; A0A109ULB8; -.
DR   STRING; 507626.LOKO_01156; -.
DR   KEGG; hco:LOKO_01156; -.
DR   PATRIC; fig|507626.3.peg.1145; -.
DR   OrthoDB; 9762536at2; -.
DR   Proteomes; UP000063387; 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:AMD00229.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063387};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT   DOMAIN          48..191
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          217..275
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          284..336
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT   SITE            66
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            118
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            159
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            200
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ   SEQUENCE   336 AA;  35265 MW;  AFB147299E4D3B96 CRC64;
     MTIDAASPHQ ADPADVSPLR DSARRTLQIE HQAIGALADR LDSHFDHACE LMLACQGRVV
     VTGMGKSGHI AGKIAATLAS TGTPAFFVHP GEASHGDLGM ITPGDVVLAL SNSGETGEVT
     AILPLLKRMG TPLVSMTGNP ESTLARHADA HLSAAVAREA CPLDLAPTAS TTAALALGDA
     LAVALLEARG FTAEDFARSH PGGSLGKRLL LRVADLMHQG TRLPSVPMGS PLRDALLEMS
     RQGLGFTCVV DVQNRLIGVY TDGDLRRTLD QHTDLSQLSV DDVMTRPGKR IAPDLLAAEA
     VRVMEDNRIT ALAVVDEEGH PVGALHMHDL LRSGVI
//
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