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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)DescriptionActionsGraphical viewLength
Binding sitei319Substrate1
Metal bindingi496Zinc; catalytic1
Active sitei497Proton acceptorCurated1
Metal bindingi500Zinc; catalytic1
Metal bindingi519Zinc; catalytic1
Sitei580Transition state stabilizerCurated1

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 databases

ChEMBLiCHEMBL4117.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000951001 – 1085M1 family aminopeptidaseAdd BLAST1085

Post-translational modificationi

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

Proteomic databases

PRIDEiO96935.

Expressioni

Developmental stagei

Expressed in all erythrocytic stages.2 Publications

Interactioni

Chemistry databases

BindingDBiO96935.

Structurei

Secondary structure

11085
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi201 – 203Combined sources3
Beta strandi208 – 220Combined sources13
Beta strandi225 – 235Combined sources11
Beta strandi244 – 247Combined sources4
Beta strandi252 – 258Combined sources7
Turni266 – 268Combined sources3
Beta strandi269 – 271Combined sources3
Beta strandi273 – 278Combined sources6
Helixi280 – 282Combined sources3
Beta strandi285 – 296Combined sources12
Helixi298 – 300Combined sources3
Beta strandi305 – 310Combined sources6
Beta strandi313 – 317Combined sources5
Turni319 – 322Combined sources4
Helixi323 – 325Combined sources3
Beta strandi337 – 346Combined sources10
Turni347 – 349Combined sources3
Beta strandi352 – 365Combined sources14
Turni366 – 368Combined sources3
Beta strandi369 – 380Combined sources12
Helixi382 – 384Combined sources3
Beta strandi387 – 390Combined sources4
Beta strandi392 – 400Combined sources9
Beta strandi402 – 404Combined sources3
Beta strandi407 – 415Combined sources9
Helixi416 – 422Combined sources7
Helixi423 – 440Combined sources18
Beta strandi446 – 455Combined sources10
Beta strandi458 – 462Combined sources5
Beta strandi467 – 471Combined sources5
Helixi472 – 474Combined sources3
Turni479 – 481Combined sources3
Helixi485 – 499Combined sources15
Turni500 – 502Combined sources3
Turni504 – 506Combined sources3
Beta strandi507 – 511Combined sources5
Helixi512 – 514Combined sources3
Helixi515 – 534Combined sources20
Helixi538 – 555Combined sources18
Beta strandi566 – 569Combined sources4
Helixi571 – 574Combined sources4
Helixi577 – 610Combined sources34
Beta strandi613 – 615Combined sources3
Helixi617 – 631Combined sources15
Helixi641 – 643Combined sources3
Helixi644 – 647Combined sources4
Beta strandi653 – 661Combined sources9
Turni662 – 665Combined sources4
Beta strandi666 – 674Combined sources9
Beta strandi689 – 696Combined sources8
Turni698 – 700Combined sources3
Beta strandi708 – 712Combined sources5
Beta strandi714 – 723Combined sources10
Beta strandi729 – 733Combined sources5
Beta strandi738 – 743Combined sources6
Helixi748 – 757Combined sources10
Helixi761 – 789Combined sources29
Helixi801 – 811Combined sources11
Helixi818 – 824Combined sources7
Helixi830 – 833Combined sources4
Helixi834 – 836Combined sources3
Beta strandi838 – 840Combined sources3
Helixi842 – 870Combined sources29
Helixi872 – 875Combined sources4
Turni879 – 882Combined sources4
Helixi889 – 907Combined sources19
Helixi913 – 920Combined sources8
Helixi926 – 935Combined sources10
Helixi936 – 938Combined sources3
Helixi942 – 953Combined sources12
Helixi957 – 968Combined sources12
Helixi975 – 985Combined sources11
Turni986 – 989Combined sources4
Helixi993 – 1004Combined sources12
Helixi1007 – 1010Combined sources4
Helixi1016 – 1029Combined sources14
Helixi1033 – 1039Combined sources7
Helixi1040 – 1048Combined sources9
Helixi1051 – 1065Combined sources15
Helixi1072 – 1081Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO96935.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni460 – 464Substrate binding5

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Family and domain databases

CDDicd09600. M1_APN_1. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiO96935.
ChEMBLiCHEMBL4117.

Protein family/group databases

MEROPSiM01.029.

Proteomic databases

PRIDEiO96935.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.11.20. 4889.

Miscellaneous databases

EvolutionaryTraceiO96935.

Family and domain databases

CDDicd09600. M1_APN_1. 1 hit.
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...

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: November 2, 2016
This is version 100 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.