Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P44009

- APHA_HAEIN

UniProt

P44009 - APHA_HAEIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Class B acid phosphatase

Gene

aphA

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Dephosphorylates several organic phosphate monoesters. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds (By similarity).By similarity

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactori

Binds 1 magnesium ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei67 – 671NucleophileBy similarity
Metal bindingi67 – 671MagnesiumBy similarity
Active sitei69 – 691Proton donorBy similarity
Metal bindingi69 – 691Magnesium; via carbonyl oxygenBy similarity
Binding sitei176 – 1761SubstrateBy similarity
Metal bindingi191 – 1911MagnesiumBy similarity

GO - Molecular functioni

  1. acid phosphatase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Class B acid phosphatase (EC:3.1.3.2)
Short name:
CBAP
Gene namesi
Name:aphA
Synonyms:napA
Ordered Locus Names:HI_0494/HI_0495
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579: Chromosome

Subcellular locationi

Periplasm By similarity

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 236214Class B acid phosphatasePRO_0000024005Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi71421.HI0495m.

Structurei

3D structure databases

ProteinModelPortaliP44009.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni136 – 1372Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3700.
KOiK03788.
OrthoDBiEOG6HTNVZ.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR005519. Acid_phosphat_B.
IPR023214. HAD-like_dom.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view]
PfamiPF03767. Acid_phosphat_B. 1 hit.
[Graphical view]
PIRSFiPIRSF017818. Acid_Ptase_B. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01672. AphA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P44009-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKNVMKLSVI ALLTAAAVPA MAGKTEPYTQ SGTNAREMLQ EQAIHWISVD
60 70 80 90 100
QIKQSLEGKA PINVSFDIDD TVMLFSSPCF YHGQQKFSPG KHDYLKNQDF
110 120 130 140 150
WNEVNAGCDK YSIPKQIAID LINMHQARGD QVYFFTGRTA GKVDGVTPIL
160 170 180 190 200
EKTFNIKNMH PVEFMGSRER TTKYNKTPAI ISHKVSIHYG DSDDDVLAAK
210 220 230
EAGVRGIRLM RAANSTYQPM PTLGGYGEEV LINSSY
Length:236
Mass (Da):26,271
Last modified:November 1, 1995 - v1
Checksum:iD5D7091AC6BB4418
GO

Sequence cautioni

The sequence AAC22151.1 differs from that shown. Reason: Frameshift at position 66. Produces two separate ORFs.
The sequence AAC22152.1 differs from that shown. Reason: Frameshift at position 66. Produces two separate ORFs.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731Missing in CAA68889. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC22151.1. Frameshift.
L42023 Genomic DNA. Translation: AAC22152.1. Frameshift.
Y07615 Genomic DNA. Translation: CAA68889.1.
PIRiT09434.
RefSeqiNP_438653.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22151; AAC22151; HI_0494.
AAC22152; AAC22152; HI_0495.
GeneIDi950561.
KEGGihin:HI0495m.
PATRICi20189539. VBIHaeInf48452_0512.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC22151.1 . Frameshift.
L42023 Genomic DNA. Translation: AAC22152.1 . Frameshift.
Y07615 Genomic DNA. Translation: CAA68889.1 .
PIRi T09434.
RefSeqi NP_438653.1. NC_000907.1.

3D structure databases

ProteinModelPortali P44009.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 71421.HI0495m.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC22151 ; AAC22151 ; HI_0494 .
AAC22152 ; AAC22152 ; HI_0495 .
GeneIDi 950561.
KEGGi hin:HI0495m.
PATRICi 20189539. VBIHaeInf48452_0512.

Phylogenomic databases

eggNOGi COG3700.
KOi K03788.
OrthoDBi EOG6HTNVZ.

Family and domain databases

Gene3Di 3.40.50.1000. 1 hit.
InterProi IPR005519. Acid_phosphat_B.
IPR023214. HAD-like_dom.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view ]
Pfami PF03767. Acid_phosphat_B. 1 hit.
[Graphical view ]
PIRSFi PIRSF017818. Acid_Ptase_B. 1 hit.
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01672. AphA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. Rossolini G.M., Bonci A., Schippa S., Iori P., Thaller M.C.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CCUG 7317/A.
  3. "Two-dimensional map of the proteome of Haemophilus influenzae."
    Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C., Fountoulakis M.
    Electrophoresis 21:411-429(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Entry informationi

Entry nameiAPHA_HAEIN
AccessioniPrimary (citable) accession number: P44009
Secondary accession number(s): P44730, P77869
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 1, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3