ALPH_ELIME
ID ALPH_ELIME Reviewed; 546 AA.
AC Q9KJX5;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Alkaline phosphatase PafA {ECO:0000303|PubMed:11577161, ECO:0000312|EMBL:AAF80345.1};
DE Short=AP PafA {ECO:0000303|PubMed:11577161};
DE EC=3.1.3.1 {ECO:0000269|PubMed:11577161};
DE Flags: Precursor;
GN Name=pafA {ECO:0000312|EMBL:AAF80345.1};
OS Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=238;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF80345.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP AND INDUCTION.
RC STRAIN=ATCC 13254 / CCUG 4310 / CIP 6058 / LMG 12280 / NCTC 10585
RC {ECO:0000312|EMBL:AAF80345.1};
RX PubMed=11577161; DOI=10.1099/00221287-147-10-2831;
RA Berlutti F., Passariello C., Selan L., Thaller M.C., Rossolini G.M.;
RT "The Chryseobacterium meningosepticum PafA enzyme: prototype of a new
RT enzyme family of prokaryotic phosphate-irrepressible alkaline
RT phosphatases?";
RL Microbiology 147:2831-2839(2001).
CC -!- FUNCTION: Alkaline phosphatase with broad substrate specificity. Has
CC phosphatase activity towards nucleotide phosphates with a preference
CC for ATP. Active towards a great variety of phosphomonoesters with the
CC exception of 2',3'-cyclic AMP and myo-inositol hexakisphosphate.
CC {ECO:0000269|PubMed:11577161}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC Evidence={ECO:0000269|PubMed:11577161};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:A1YYW7};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:A1YYW7};
CC -!- ACTIVITY REGULATION: Strongly inhibited by orthovanadate and EDTA. Also
CC inhibited by inorganic phosphate. {ECO:0000269|PubMed:11577161}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=115 uM for 4-nitrophenyl phosphate {ECO:0000269|PubMed:11577161};
CC KM=74 uM for 3'-AMP {ECO:0000269|PubMed:11577161};
CC KM=90 uM for 5'-AMP {ECO:0000269|PubMed:11577161};
CC KM=35 uM for ADP {ECO:0000269|PubMed:11577161};
CC KM=10 uM for ATP {ECO:0000269|PubMed:11577161};
CC pH dependence:
CC Optimum pH is 8.5 with 4-nitrophenyl phosphate as substrate. Has 50%
CC residual activity at pH 7.5 and 30% at pH 9.0, being virtually
CC inactive at pH 10 and at pH 5 or lower.
CC {ECO:0000269|PubMed:11577161};
CC Temperature dependence:
CC Heat-labile. Incubation for 10 minutes at 50 or 60 degrees Celsius
CC causes 40% and 60% inactivation, respectively. Heating at 100 degrees
CC Celsius for 2 minutes causes total loss of activity. Heat-inactivated
CC enzyme cannot be renaturated. {ECO:0000269|PubMed:11577161};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11577161}.
CC -!- INDUCTION: Expression is not repressed by inorganic phosphate.
CC {ECO:0000269|PubMed:11577161}.
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DR EMBL; AF157621; AAF80345.1; -; Genomic_DNA.
DR PDB; 5TJ3; X-ray; 1.70 A; A=21-546.
DR PDB; 5TOO; X-ray; 1.70 A; A=21-546.
DR PDBsum; 5TJ3; -.
DR PDBsum; 5TOO; -.
DR AlphaFoldDB; Q9KJX5; -.
DR SMR; Q9KJX5; -.
DR STRING; 1216967.L100_07644; -.
DR eggNOG; COG1524; Bacteria.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:UniProtKB.
DR GO; GO:0019203; F:carbohydrate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008877; F:glucose-1-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IDA:UniProtKB.
DR GO; GO:0050308; F:sugar-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR CDD; cd16016; AP-SPAP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR026263; Alkaline_phosphatase_prok.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR Pfam; PF01663; Phosphodiest; 1.
DR PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Periplasm; Phosphoprotein; Signal;
KW Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..546
FT /note="Alkaline phosphatase PafA"
FT /evidence="ECO:0000255"
FT /id="PRO_0000425536"
FT ACT_SITE 79
FT /note="Phosphothreonine intermediate"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 162..164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:5TJ3"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:5TJ3"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:5TJ3"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:5TJ3"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:5TJ3"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 269..285
FT /evidence="ECO:0007829|PDB:5TJ3"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 316..339
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 416..428
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 451..458
FT /evidence="ECO:0007829|PDB:5TJ3"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:5TJ3"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:5TJ3"
FT HELIX 519..527
FT /evidence="ECO:0007829|PDB:5TJ3"
FT TURN 541..543
FT /evidence="ECO:0007829|PDB:5TJ3"
SQ SEQUENCE 546 AA; 60753 MW; 1A2CB1435BC74BD2 CRC64;
MLTPKKWLLG VLVVSGMLGA QKTNAVPRPK LVVGLVVDQM RWDYLYRYYS KYGEGGFKRM
LNTGYSLNNV HIDYVPTVTA IGHTSIFTGS VPSIHGIAGN DWYDKELGKS VYCTSDETVQ
PVGTTSNSVG QHSPRNLWST TVTDQLGLAT NFTSKVVGVS LKDRASILPA GHNPTGAFWF
DDTTGKFITS TYYTKELPKW VNDFNNKNVP AQLVANGWNT LLPINQYTES SEDNVEWEGL
LGSKKTPTFP YTDLAKDYEA KKGLIRTTPF GNTLTLQMAD AAIDGNQMGV DDITDFLTVN
LASTDYVGHN FGPNSIEVED TYLRLDRDLA DFFNNLDKKV GKGNYLVFLS ADHGAAHSVG
FMQAHKMPTG FFVEDMKKEM NAKLKQKFGA DNIIAAAMNY QVYFDRKVLA DSKLELDDVR
DYVMTELKKE PSVLYVLSTD EIWESSIPEP IKSRVINGYN WKRSGDIQII SKDGYLSAYS
KKGTTHSVWN SYDSHIPLLF MGWGIKQGES NQPYHMTDIA PTVSSLLKIQ FPSGAVGKPI
TEVIGR
