API_HAEIN
ID API_HAEIN Reviewed; 337 AA.
AC P45313;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable arabinose 5-phosphate isomerase;
DE Short=API;
DE EC=5.3.1.13;
GN OrderedLocusNames=HI_1678;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Catalyzes the reversible aldol-ketol isomerization between D-
CC ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P).
CC {ECO:0000250}.
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;
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC23324.1; -; Genomic_DNA.
DR PIR; C64136; C64136.
DR RefSeq; NP_439820.1; NC_000907.1.
DR AlphaFoldDB; P45313; -.
DR SMR; P45313; -.
DR STRING; 71421.HI_1678; -.
DR PRIDE; P45313; -.
DR EnsemblBacteria; AAC23324; AAC23324; HI_1678.
DR KEGG; hin:HI_1678; -.
DR PATRIC; fig|71421.8.peg.1757; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR HOGENOM; CLU_040681_13_1_6; -.
DR OMA; EREVCPN; -.
DR PhylomeDB; P45313; -.
DR BioCyc; HINF71421:G1GJ1-1694-MON; -.
DR Proteomes; UP000000579; Chromosome.
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:UniProtKB-KW.
DR CDD; cd05014; SIS_Kpsf; 1.
DR Gene3D; 3.10.580.10; -; 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 Pfam; PF00571; CBS; 2.
DR Pfam; PF01380; SIS; 1.
DR PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR00393; kpsF; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; CBS domain; Isomerase; Metal-binding;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..337
FT /note="Probable arabinose 5-phosphate isomerase"
FT /id="PRO_0000136582"
FT DOMAIN 58..201
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 227..284
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 292..337
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 92..93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131..140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165..167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 76
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 128
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 169
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 210
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
SQ SEQUENCE 337 AA; 36655 MW; 6A12AC7A87DB061C CRC64;
MPNFSFVFFY DSAKITPIST ALLGRRMNYL KIAQDSLSVE SNALLQLSQR LGDDFNQVID
LILACEGRLV IGGIGKSGLI GKKMVATFAS TGTPSFFLHP TEAFHGDLGM LKPIDIVMLI
SYSGETDDVN KLIPSLKNFG NKIIAVTSNK NSTLARHADY VLDITVEREV CPNNLAPTTS
ALVTLALGDA LAVSLITARN FQPADFAKFH PGGSLGRRLL CKVKDQMQTR LPTILPTTNF
TDCLTVMNEG RMGVALVMEN EQLKGIITDG DIRRALTANG AGTLNKTAKD FMTSSPKTIH
QDEFLSKAED FMKAKKIHSL VVVNDENHVV GLVEFSS
