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Protein

M1 family aminopeptidase

Gene
N/A
Organism
Plasmodium falciparum (isolate FcB1 / Columbia)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC.2 Publications

Cofactori

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit.2 Publications

Enzyme regulationi

Inhibited by 1,10-phenanthroline, EDTA and bestatin. Activity is not affected by phosphoramidin, PMSF, leupeptin, iodoacetamide or pepstatin.2 Publications

pH dependencei

Optimum pH is 7.4. Active from pH 5.8 to 8.6, with less than 20% of normal activity at pH 6.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei319 – 3191Substrate
Metal bindingi496 – 4961Zinc; catalytic
Active sitei497 – 4971Proton acceptorCurated
Metal bindingi500 – 5001Zinc; catalytic
Metal bindingi519 – 5191Zinc; catalytic
Sitei580 – 5801Transition state stabilizerCurated

GO - Molecular functioni

  • aminopeptidase activity Source: UniProtKB
  • metallopeptidase activity Source: UniProtKB-KW
  • zinc ion binding Source: InterPro

GO - Biological processi

  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.11.20. 4889.

Protein family/group databases

MEROPSiM01.029.

Names & Taxonomyi

Protein namesi
Recommended name:
M1 family aminopeptidase (EC:3.4.11.-)
Alternative name(s):
Pfa-M1
OrganismiPlasmodium falciparum (isolate FcB1 / Columbia)
Taxonomic identifieri186763 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4117.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10851085M1 family aminopeptidasePRO_0000095100Add
BLAST

Post-translational modificationi

The 120 kDa precursor is cleaved in vitro into 96 kDa and 68 kDa forms.

Expressioni

Developmental stagei

Expressed in all erythrocytic stages.2 Publications

Interactioni

Chemistry

BindingDBiO96935.

Structurei

Secondary structure

1
1085
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi201 – 2033Combined sources
Beta strandi208 – 22013Combined sources
Beta strandi225 – 23511Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi252 – 2587Combined sources
Turni266 – 2683Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi273 – 2786Combined sources
Helixi280 – 2823Combined sources
Beta strandi285 – 29612Combined sources
Helixi298 – 3003Combined sources
Beta strandi305 – 3106Combined sources
Beta strandi313 – 3175Combined sources
Turni319 – 3224Combined sources
Helixi323 – 3253Combined sources
Beta strandi337 – 34610Combined sources
Turni347 – 3493Combined sources
Beta strandi352 – 36514Combined sources
Turni366 – 3683Combined sources
Beta strandi369 – 38012Combined sources
Helixi382 – 3843Combined sources
Beta strandi387 – 3904Combined sources
Beta strandi392 – 4009Combined sources
Beta strandi402 – 4043Combined sources
Beta strandi407 – 4159Combined sources
Helixi416 – 4227Combined sources
Helixi423 – 44018Combined sources
Beta strandi446 – 45510Combined sources
Beta strandi458 – 4625Combined sources
Beta strandi467 – 4715Combined sources
Helixi472 – 4743Combined sources
Turni479 – 4813Combined sources
Helixi485 – 49915Combined sources
Turni500 – 5023Combined sources
Turni504 – 5063Combined sources
Beta strandi507 – 5115Combined sources
Helixi512 – 5143Combined sources
Helixi515 – 53420Combined sources
Helixi538 – 55518Combined sources
Beta strandi566 – 5694Combined sources
Helixi571 – 5744Combined sources
Helixi577 – 61034Combined sources
Beta strandi613 – 6153Combined sources
Helixi617 – 63115Combined sources
Helixi641 – 6433Combined sources
Helixi644 – 6474Combined sources
Beta strandi653 – 6619Combined sources
Turni662 – 6654Combined sources
Beta strandi666 – 6749Combined sources
Beta strandi689 – 6968Combined sources
Turni698 – 7003Combined sources
Beta strandi708 – 7125Combined sources
Beta strandi714 – 72310Combined sources
Beta strandi729 – 7335Combined sources
Beta strandi738 – 7436Combined sources
Helixi748 – 75710Combined sources
Helixi761 – 78929Combined sources
Helixi801 – 81111Combined sources
Helixi818 – 8247Combined sources
Helixi830 – 8334Combined sources
Helixi834 – 8363Combined sources
Beta strandi838 – 8403Combined sources
Helixi842 – 87029Combined sources
Helixi872 – 8754Combined sources
Turni879 – 8824Combined sources
Helixi889 – 90719Combined sources
Helixi913 – 9208Combined sources
Helixi926 – 93510Combined sources
Helixi936 – 9383Combined sources
Helixi942 – 95312Combined sources
Helixi957 – 96812Combined sources
Helixi975 – 98511Combined sources
Turni986 – 9894Combined sources
Helixi993 – 100412Combined sources
Helixi1007 – 10104Combined sources
Helixi1016 – 102914Combined sources
Helixi1033 – 10397Combined sources
Helixi1040 – 10489Combined sources
Helixi1051 – 106515Combined sources
Helixi1072 – 108110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EBGX-ray2.10A196-1084[»]
3EBHX-ray1.65A196-1084[»]
3EBIX-ray2.00A195-1084[»]
3Q43X-ray1.80A195-1085[»]
3Q44X-ray1.80A195-1085[»]
3T8VX-ray1.80A196-1084[»]
4J3BX-ray2.20A197-1085[»]
4K5LX-ray1.91A195-1085[»]
4K5MX-ray1.75A195-1085[»]
4K5NX-ray1.91A196-1084[»]
4K5OX-ray1.90A196-1084[»]
4K5PX-ray1.85A196-1084[»]
4R5TX-ray1.98A196-1084[»]
4R5VX-ray2.10A196-1084[»]
4R5XX-ray1.85A182-1084[»]
4X2UX-ray1.60A196-1084[»]
4ZW3X-ray1.80A195-1084[»]
4ZW5X-ray1.80A195-1084[»]
4ZW6X-ray1.90A195-1084[»]
4ZW7X-ray1.95A195-1084[»]
4ZW8X-ray2.00A195-1084[»]
4ZX3X-ray2.00A195-1084[»]
4ZX4X-ray1.90A195-1084[»]
4ZX5X-ray1.95A195-1084[»]
4ZX6X-ray2.05A195-1084[»]
ProteinModelPortaliO96935.
SMRiO96935. Positions 197-1084.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO96935.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni460 – 4645Substrate binding

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Family and domain databases

Gene3Di1.25.50.10. 1 hit.
InterProiIPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
IPR012779. Peptidase_M1_pepN.
IPR024601. Peptidase_M1_pepN_C.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PfamiPF11940. DUF3458. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
TIGRFAMsiTIGR02414. pepN_proteo. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O96935-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLTKGCAYK YIIFTVLILA NILYDNKKRC MIKKNLRISS CGIISRLLKS
60 70 80 90 100
NSNYNSFNKN YNFTSAISEL QFSNFWNLDI LQKDIFSNIH NNKNKPQSYI
110 120 130 140 150
IHKRLMSEKG DNNNNNHQNN NGNDNKKRLG SVVNNEENTC SDKRMKPFEE
160 170 180 190 200
GHGITQVDKM NNNSDHLQQN GVMNLNSNNV ENNNNNNSVV VKKNEPKIHY
210 220 230 240 250
RKDYKPSGFI INNVTLNINI HDNETIVRSV LDMDISKHNV GEDLVFDGVG
260 270 280 290 300
LKINEISINN KKLVEGEEYT YDNEFLTIFS KFVPKSKFAF SSEVIIHPET
310 320 330 340 350
NYALTGLYKS KNIIVSQCEA TGFRRITFFI DRPDMMAKYD VTVTADKEKY
360 370 380 390 400
PVLLSNGDKV NEFEIPGGRH GARFNDPHLK PCYLFAVVAG DLKHLSATYI
410 420 430 440 450
TKYTKKKVEL YVFSEEKYVS KLQWALECLK KSMAFDEDYF GLEYDLSRLN
460 470 480 490 500
LVAVSDFNVG AMENKGLNIF NANSLLASKK NSIDFSYARI LTVVGHEYFH
510 520 530 540 550
NYTGNRVTLR DWFQLTLKEG LTVHRENLFS EEMTKTVTTR LSHVDLLRSV
560 570 580 590 600
QFLEDSSPLS HPIRPESYVS MENFYTTTVY DKGSEVMRMY LTILGEEYYK
610 620 630 640 650
KGFDIYIKKN DGNTATCEDF NYAMEQAYKM KKADNSANLN QYLLWFSQSG
660 670 680 690 700
TPHVSFKYNY DAEKKQYSIH VNQYTKPDEN QKEKKPLFIP ISVGLINPEN
710 720 730 740 750
GKEMISQTTL ELTKESDTFV FNNIAVKPIP SLFRGFSAPV YIEDNLTDEE
760 770 780 790 800
RILLLKYDSD AFVRYNSCTN IYMKQILMNY NEFLKAKNEK LESFNLTPVN
810 820 830 840 850
AQFIDAIKYL LEDPHADAGF KSYIVSLPQD RYIINFVSNL DTDVLADTKE
860 870 880 890 900
YIYKQIGDKL NDVYYKMFKS LEAKADDLTY FNDESHVDFD QMNMRTLRNT
910 920 930 940 950
LLSLLSKAQY PNILNEIIEH SKSPYPSNWL TSLSVSAYFD KYFELYDKTY
960 970 980 990 1000
KLSKDDELLL QEWLKTVSRS DRKDIYEILK KLENEVLKDS KNPNDIRAVY
1010 1020 1030 1040 1050
LPFTNNLRRF HDISGKGYKL IAEVITKTDK FNPMVATQLC EPFKLWNKLD
1060 1070 1080
TKRQELMLNE MNTMLQEPNI SNNLKEYLLR LTNKL
Length:1,085
Mass (Da):126,062
Last modified:May 30, 2003 - v2
Checksum:i72AE30928D6BD550
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09081 Genomic DNA. Translation: CAA70301.2.
PIRiT28636.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09081 Genomic DNA. Translation: CAA70301.2.
PIRiT28636.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EBGX-ray2.10A196-1084[»]
3EBHX-ray1.65A196-1084[»]
3EBIX-ray2.00A195-1084[»]
3Q43X-ray1.80A195-1085[»]
3Q44X-ray1.80A195-1085[»]
3T8VX-ray1.80A196-1084[»]
4J3BX-ray2.20A197-1085[»]
4K5LX-ray1.91A195-1085[»]
4K5MX-ray1.75A195-1085[»]
4K5NX-ray1.91A196-1084[»]
4K5OX-ray1.90A196-1084[»]
4K5PX-ray1.85A196-1084[»]
4R5TX-ray1.98A196-1084[»]
4R5VX-ray2.10A196-1084[»]
4R5XX-ray1.85A182-1084[»]
4X2UX-ray1.60A196-1084[»]
4ZW3X-ray1.80A195-1084[»]
4ZW5X-ray1.80A195-1084[»]
4ZW6X-ray1.90A195-1084[»]
4ZW7X-ray1.95A195-1084[»]
4ZW8X-ray2.00A195-1084[»]
4ZX3X-ray2.00A195-1084[»]
4ZX4X-ray1.90A195-1084[»]
4ZX5X-ray1.95A195-1084[»]
4ZX6X-ray2.05A195-1084[»]
ProteinModelPortaliO96935.
SMRiO96935. Positions 197-1084.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiO96935.
ChEMBLiCHEMBL4117.

Protein family/group databases

MEROPSiM01.029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.11.20. 4889.

Miscellaneous databases

EvolutionaryTraceiO96935.

Family and domain databases

Gene3Di1.25.50.10. 1 hit.
InterProiIPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
IPR012779. Peptidase_M1_pepN.
IPR024601. Peptidase_M1_pepN_C.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PfamiPF11940. DUF3458. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
TIGRFAMsiTIGR02414. pepN_proteo. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A Plasmodium falciparum aminopeptidase gene belonging to the M1 family of zinc-metallopeptidases is expressed in erythrocytic stages."
    Florent I.C.P., Derhy Z., Allary M., Monsigny M., Mayer R., Schrevel J.
    Mol. Biochem. Parasitol. 97:149-160(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  2. Florent I.C.P.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO N-TERMINUS.
  3. "Properties, stage-dependent expression and localization of Plasmodium falciparum M1 family zinc-aminopeptidase."
    Allary M., Schrevel J., Florent I.C.P.
    Parasitology 125:1-10(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 196-1084 IN COMPLEX WITH ZINC IONS AND BESTATIN, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  5. "Synthesis of new (-)-bestatin-based inhibitor libraries reveals a novel binding mode in the s1 pocket of the essential malaria m1 metalloaminopeptidase."
    Velmourougane G., Harbut M.B., Dalal S., McGowan S., Oellig C.A., Meinhardt N., Whisstock J.C., Klemba M., Greenbaum D.C.
    J. Med. Chem. 54:1655-1666(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 195-1085 IN COMPLEX WITH ZINC IONS AND SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, COFACTOR.

Entry informationi

Entry nameiAMP1_PLAFQ
AccessioniPrimary (citable) accession number: O96935
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: May 30, 2003
Last modified: May 11, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.