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Database: UniProt
Entry: F5S127_9ENTR
LinkDB: F5S127_9ENTR
Original site: F5S127_9ENTR 
ID   F5S127_9ENTR            Unreviewed;       321 AA.
AC   F5S127;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
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:EGK58001.1};
GN   ORFNames=HMPREF9086_3587 {ECO:0000313|EMBL:EGK58001.1};
OS   Enterobacter hormaechei ATCC 49162.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=888063 {ECO:0000313|EMBL:EGK58001.1, ECO:0000313|Proteomes:UP000002984};
RN   [1] {ECO:0000313|EMBL:EGK58001.1, ECO:0000313|Proteomes:UP000002984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49162 {ECO:0000313|EMBL:EGK58001.1,
RC   ECO:0000313|Proteomes:UP000002984};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (APR-2011) 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   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:EGK58001.1}.
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DR   EMBL; AFHR01000063; EGK58001.1; -; Genomic_DNA.
DR   RefSeq; WP_006811723.1; NZ_MKEQ01000002.1.
DR   AlphaFoldDB; F5S127; -.
DR   HOGENOM; CLU_040681_13_1_6; -.
DR   Proteomes; UP000002984; 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:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
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:SF2; ARABINOSE 5-PHOSPHATE ISOMERASE GUTQ; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF01380; SIS; 1.
DR   PIRSF; PIRSF004692; KdsD_KpsF; 1.
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:EGK58001.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT   DOMAIN          34..177
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          203..263
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          269..321
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT   SITE            52
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            104
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            145
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT   SITE            186
FT                   /note="Catalytically relevant"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ   SEQUENCE   321 AA;  34254 MW;  4F4EE918B3AA9F45 CRC64;
     MSDFLLNAGR QTLLLELQEA SRLPERLGED FVRAANTIIH CEGKVIVAGI GKSGHIGKKI
     AATLASTGTP AFFVHPAEAL HGDLGMIESR DVMLFISYSG SAKELDLIIP RLQEKSVALL
     AMTGKSRSPL ALAAKATLDI SVEREACPMH LAPTSSTVNT LMMGDALAMA VMQARGFNEE
     DFARSHPAGA LGARLLNKVH HLMRTDDAIP QVKLDTSVMD AMLELSRTGL GLVAVCDDGG
     NVKGVFTDGD LRRWLVGGGR LETQVSDAMT KGGLTLNADS RAIEAKEVLM KRKITAAPVV
     DEHGRLCGAI NLQDFYQAGI I
//
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