ID A0A101VM28_9SPHN Unreviewed; 335 AA.
AC A0A101VM28;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE SubName: Full=D-arabinose 5-phosphate {ECO:0000313|EMBL:KUO57297.1};
GN ORFNames=APF82_01980 {ECO:0000313|EMBL:KUO57297.1};
OS Sphingomonadales bacterium BRH_c42.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX NCBI_TaxID=1734407 {ECO:0000313|EMBL:KUO57297.1, ECO:0000313|Proteomes:UP000054281};
RN [1] {ECO:0000313|EMBL:KUO57297.1, ECO:0000313|Proteomes:UP000054281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c42 {ECO:0000313|EMBL:KUO57297.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-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:KUO57297.1}.
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DR EMBL; LOEX01000012; KUO57297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101VM28; -.
DR Proteomes; UP000054281; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; 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 Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 45..188
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 213..275
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 277..335
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 63
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 115
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 156
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 197
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 335 AA; 35014 MW; F7928C68EF3BA6B5 CRC64;
MAVGLADRAT SSRESHIAVG RDVIGLEADA LVELNGQIGD EFAQAVEMIL GCKQRVIVSG
IGKSGHIARK IAATLAATGT PALFVHAAEA AHGDVGMVSR GDLLIVFSNS GATVEVQPLC
IYAKTIGCPL IGVSRNPNSL LMRTADLGLC LPKIEEVCTS SLAPTTSSTM MLALGDALAV
ATMRARGISG PDIRLFHTGG AIGLQLRGVE DVMHSGERLP LVGLETPMPD VLVTMTEKRL
GMAGVVDAAG ELVGVITDGD LRRHARNLVF NTAAEVMSHA PRTINSGATV QEALELMNTH
RITVLFVVNE RQPRIPLGVV QIYDIAAPPS TVVAP
//
