ID A0A363UM78_9GAMM Unreviewed; 326 AA.
AC A0A363UM78;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ORFNames=DEH80_06820 {ECO:0000313|EMBL:PWN56538.1};
OS Abyssibacter profundi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Abyssibacter.
OX NCBI_TaxID=2182787 {ECO:0000313|EMBL:PWN56538.1, ECO:0000313|Proteomes:UP000251800};
RN [1] {ECO:0000313|EMBL:PWN56538.1, ECO:0000313|Proteomes:UP000251800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUC007 {ECO:0000313|EMBL:PWN56538.1,
RC ECO:0000313|Proteomes:UP000251800};
RA Zhou S.;
RT "Abyssibacter profundi OUC007T gen. nov., sp. nov, a marine bacterium
RT isolated from seawater of the Mariana Trench.";
RL Submitted (MAY-2018) 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 -!- 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:PWN56538.1}.
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DR EMBL; QEQK01000005; PWN56538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A363UM78; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000251800; 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; 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:PWN56538.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000251800};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 38..181
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 207..265
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 274..326
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 56
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 108
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 149
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 190
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 326 AA; 34424 MW; 6A8B961B2AD17F2F CRC64;
MTTLHPDQIR ALGVSVLRIE RDAIERLVDR IDEAFVRACE LCIGCSARIV VVGMGKSGHI
GNKIAATLAS TGTPAFFVHP GEASHGDLGM ITRDDVVLAL SNSGETAEIT AILPLIKRLG
VPLIAMTGKP ESTLARMADV HLNVGVEKEA CPLNLAPTAS TTAALAMGDA LAVALLEARG
FTESDFALSH PGGSLGRRLL LKIDELLHTG ERIPRVGATV TVAEALVEMT QKGLGMTVVD
DADGHMLGIY TDGDLRRTLD RGLDVHATPI TEVMAADPKS IAPGTLAAEA VKIMQDFSIT
TLVVCDEQRR VTGLLHMHEL LRAGVV
//
