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Database: UniProt
Entry: Q47VI6_COLP3
LinkDB: Q47VI6_COLP3
Original site: Q47VI6_COLP3 
ID   Q47VI6_COLP3            Unreviewed;       321 AA.
AC   Q47VI6;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 98.
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   OrderedLocusNames=CPS_4538 {ECO:0000313|EMBL:AAZ26760.1};
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ26760.1, ECO:0000313|Proteomes:UP000000547};
RN   [1] {ECO:0000313|EMBL:AAZ26760.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H {ECO:0000313|EMBL:AAZ26760.1};
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ26760.1; -; Genomic_DNA.
DR   RefSeq; WP_011045267.1; NC_003910.7.
DR   AlphaFoldDB; Q47VI6; -.
DR   STRING; 167879.CPS_4538; -.
DR   KEGG; cps:CPS_4538; -.
DR   eggNOG; COG0517; Bacteria.
DR   eggNOG; COG0794; Bacteria.
DR   HOGENOM; CLU_040681_13_1_6; -.
DR   OMA; LMACLMR; -.
DR   Proteomes; UP000000547; 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};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT   DOMAIN          33..176
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          202..260
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          269..321
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT   SITE            51
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            103
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            144
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            185
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ   SEQUENCE   321 AA;  34242 MW;  B122E044731E62A8 CRC64;
     MKNFKELAKN VIEIEQQAIA ELVQFIDDNF ELACQLMFHC KGRVIVIGMG KSGHIGGKIA
     ATLASTGTPS FFVHPGEASH GDLGMVTSND VVLTISNSGE TSEVLAIIPV IKRIGAKLIS
     MTGNTESTLA KLADTHVCIK VSAEACPLGL TPTSSTTATL VMGDALAVAL LNARDFTAED
     FALSHPGGSL GKRLLLRLSD IMHKDDRVPM ISENALIKDA LVEMSLKGLG MTAIVNEQQQ
     LVGLFTDGDL RRVLDNRIDI HSESINTVMT HNPSVAQSDM LAAQALKIME DKKINGLIIV
     DSNNIPVGAM NMHDFLSSGV L
//
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