ID A0A0Q7SDQ8_9BURK Unreviewed; 328 AA.
AC A0A0Q7SDQ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Arabinose 5-phosphate isomerase {ECO:0000313|EMBL:KQY86197.1};
GN ORFNames=ASD35_21500 {ECO:0000313|EMBL:KQY86197.1};
OS Pelomonas sp. Root1444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1736464 {ECO:0000313|EMBL:KQY86197.1, ECO:0000313|Proteomes:UP000051648};
RN [1] {ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|Proteomes:UP000051648};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY86197.1, ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|EMBL:KQY86197.1,
RC ECO:0000313|Proteomes:UP000051648};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQY86197.1}.
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DR EMBL; LMFP01000011; KQY86197.1; -; Genomic_DNA.
DR RefSeq; WP_056875342.1; NZ_LMFP01000011.1.
DR AlphaFoldDB; A0A0Q7SDQ8; -.
DR STRING; 1736464.ASD35_21500; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000051648; 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:KQY86197.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000051648};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 40..183
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 209..267
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 276..328
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 58
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 110
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 151
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 192
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 328 AA; 34142 MW; C1978E8F364436F5 CRC64;
MSAPPFAAER AIRMGREALA VEARALSELG PRLGEAFARA VEAMLGCRGR VAVMGMGKSG
HVGRKIAATL ASTGTPALFV HPAEAAHGDL GMVTPGDLVL ALSNSGESDE LNAILPVLKR
LGIPVVAMTG RPESSLASHA DVVLDSAVSE EACPLQLAPT ASTTAQMALG DALAVALLDA
RGFKAEDFAR SHPGGALGRK LLTHVRDLMR SGDALPRVAA TTPFTEMMRT MSAKALGLAI
VVDADDHVQG VFTDGDLRRL IEQGHDLRAL TAAEVAHPKP RTVGAEALAV DAADLMEAAR
ITVVLVVDEE RRLLGAVSIN DLMRAKVI
//
