ID A0A1G8QYD4_9RHOB Unreviewed; 324 AA.
AC A0A1G8QYD4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Arabinose-5-phosphate isomerase {ECO:0000313|EMBL:SDJ09736.1};
GN ORFNames=SAMN05421850_108148 {ECO:0000313|EMBL:SDJ09736.1};
OS Lutimaribacter saemankumensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Lutimaribacter.
OX NCBI_TaxID=490829 {ECO:0000313|EMBL:SDJ09736.1, ECO:0000313|Proteomes:UP000199340};
RN [1] {ECO:0000313|EMBL:SDJ09736.1, ECO:0000313|Proteomes:UP000199340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28010 {ECO:0000313|EMBL:SDJ09736.1,
RC ECO:0000313|Proteomes:UP000199340};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNEB01000008; SDJ09736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8QYD4; -.
DR STRING; 490829.SAMN05421850_108148; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000199340; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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:0000313|EMBL:SDJ09736.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000199340};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 41..184
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 209..266
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 271..324
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 59
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 111
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 152
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 193
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 324 AA; 33999 MW; E648A166AFC3DD9A CRC64;
MSDPSETPMR PASEVAAQVL TQEADALRLF AGAIPPDFDR VVADIARIPG RVIVSGIGKS
GHIGRKIAAT LASTGTPSYF VHASEASHGD LGMITEADIC ILISNSGETQ ELGDVVAHTR
RFSIPLVAIS SREDSTLMHA ADYRLLLPPA PEACPMGLAP TTSTTLTLAL GDALAVALME
ARDFRAENFR TFHPGGKLGA QLSTVAQLMH GGDEVPLVSI DAPMEEALLE MTSKGFGTTG
VVRNGVLAGL ISDGDLRRNM ARLMDSKAGE VATLDPVTVP PTMLAAQALA LMNARKITTL
FVVQEDGRPV GLVHLHDLLR AGVA
//
