ID A0A0J9ED06_9RHOB Unreviewed; 322 AA.
AC A0A0J9ED06;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Arabinose 5-phosphate isomerase {ECO:0000313|EMBL:KMW60566.1};
DE EC=5.3.1.13 {ECO:0000313|EMBL:KMW60566.1};
GN ORFNames=AIOL_000728 {ECO:0000313|EMBL:KMW60566.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW60566.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW60566.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW60566.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KMW60566.1}.
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DR EMBL; LFTY01000001; KMW60566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9ED06; -.
DR STRING; 1675527.AIOL_000728; -.
DR PATRIC; fig|1675527.3.peg.784; -.
DR Proteomes; UP000037178; 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; SSF54631; CBS-domain pair; 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:0000313|EMBL:KMW60566.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000037178};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 39..182
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 207..262
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 268..322
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 57
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 109
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 150
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 191
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 322 AA; 34177 MW; 3DE13EC18C7A9E87 CRC64;
MLNRMDQNKF LSTGRRVVTR EAQALHLLSS ALDDSFGQAV EMMLGATGRV IVSGMGKSGH
IARKIAATFA STGTPAHFVH PAEASHGDLG MMAQGDVALV LSNSGETAEL ADLVAYTRRF
GISLIGIASR RESTLLTQCD VCLVLPPADE ACEQGIVPTT STSMSLALGD AMAIAMMEHR
EFTPEHFRQF HPGGKLGARL SKAADLMHTD LPLVSPDTDM GEALLVMSQK GFGVLGVQDE
TGLIGVVTDG DLRRNMDGLL ERTAREVMTA EPTTIGPDAL AESAVAVMNE RRITSLFVVD
PESSRNAVGI LHVHDCLRAG IG
//
