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Entry version 19 (08 May 2019)
Sequence version 1 (16 Sep 2015)
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Protein

Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase

Gene

lnt

Organism
Mycobacterium bovis (strain BCG / Pasteur 1173P2)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.1 Publication
Transfers mannose from GDP-mannose to lipid acceptors to form polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar donor which adds mannose-phosphate residues to triacylated-phosphatidyl-myo-inositol mannosides (PIM2), eventually leading to generation of the cell wall glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM).By similarity

Miscellaneous

In a number of other Mycobacteria, including M.avis, M.leprae and M.smegmatis, these domains are encoded by 2 separate adjacent genes.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: lipoprotein biosynthesis (N-acyl transfer)

This protein is involved in the pathway lipoprotein biosynthesis (N-acyl transfer), which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway lipoprotein biosynthesis (N-acyl transfer) and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei294Proton acceptorPROSITE-ProRule annotation1
Active sitei359PROSITE-ProRule annotation1
Active sitei409NucleophilePROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Hydrolase, Transferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MBOV410289:G1G1S-2230-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00666

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase
Including the following 2 domains:
Apolipoprotein N-acyltransferase1 Publication (EC:2.3.1.2691 Publication)
Short name:
ALP N-acyltransferaseBy similarity
Polyprenol monophosphomannose synthase (EC:2.4.1.-By similarity)
Short name:
PPM synthase
Short name:
Polyprenol-P-Man synthase
Short name:
Ppm1
Alternative name(s):
Dolichol-phosphate mannose synthase (EC:2.4.1.83By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:lnt1 Publication
Synonyms:ppm1Curated
Ordered Locus Names:BCG_2070c
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMycobacterium bovis (strain BCG / Pasteur 1173P2)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri410289 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001472 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei23 – 42HelicalBy similarityAdd BLAST20
Transmembranei72 – 89HelicalBy similarityAdd BLAST18
Transmembranei94 – 115HelicalBy similarityAdd BLAST22
Transmembranei177 – 194HelicalBy similarityAdd BLAST18
Transmembranei206 – 223HelicalBy similarityAdd BLAST18
Transmembranei509 – 526HelicalBy similarityAdd BLAST18

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Loss of N-acylation of apolipoproteins.1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004345831 – 874Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthaseAdd BLAST874

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
A0A0H3M5A8

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini241 – 497CN hydrolasePROSITE-ProRule annotationAdd BLAST257

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 593Apolipoprotein N-acyltransferaseAdd BLAST593
Regioni594 – 874Polyprenol monophosphomannose synthaseAdd BLAST281

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Consists of 2 domains; the N-terminus (residues 1-593) has the N-acyltransferase activity while the C-terminus (residues 594-874) has polyprenol monophosphomannose (PPM) synthase activity.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the N-terminal section; belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily.
In the C-terminal section; belongs to the glycosyltransferase 2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K03820

Identification of Orthologs from Complete Genome Data

More...
OMAi
ADEMPND

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07571 ALP_N-acyl_transferase, 1 hit
cd06442 DPM1_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.110.10, 1 hit
3.90.550.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01148 Lnt, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004563 Apolipo_AcylTrfase
IPR003010 C-N_Hydrolase
IPR036526 C-N_Hydrolase_sf
IPR039528 DPM1-like
IPR001173 Glyco_trans_2-like
IPR029044 Nucleotide-diphossugar_trans

The PANTHER Classification System

More...
PANTHERi
PTHR43398 PTHR43398, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00795 CN_hydrolase, 1 hit
PF00535 Glycos_transf_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53448 SSF53448, 1 hit
SSF56317 SSF56317, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00546 lnt, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50263 CN_HYDROLASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

A0A0H3M5A8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLGAWVAAQ LPTTRTAVRT RLTRLVVSIV AGLLLYASFP PRNCWWAAVV
60 70 80 90 100
ALALLAWVLT HRATTPVGGL GYGLLFGLVF YVSLLPWIGE LVGPGPWLAL
110 120 130 140 150
ATTCALFPGI FGLFAVVVRL LPGWPIWFAV GWAAQEWLKS ILPFGGFPWG
160 170 180 190 200
SVAFGQAEGP LLPLVQLGGV ALLSTGVALV GCGLTAIALE IEKWWRTGGQ
210 220 230 240 250
GDAPPAVVLP AACICLVLFA AIVVWPQVRH AGSGSGGEPT VTVAVVQGNV
260 270 280 290 300
PRLGLDFNAQ RRAVLDNHVE ETLRLAADVH AGLAQQPQFV IWPENSSDID
310 320 330 340 350
PFVNPDAGQR ISAAAEAIGA PILIGTLMDV PGRPRENPEW TNTAIVWNPG
360 370 380 390 400
TGPADRHDKA IVQPFGEYLP MPWLFRHLSG YADRAGHFVP GNGTGVVRIA
410 420 430 440 450
GVPVGVATCW EVIFDRAPRK SILGGAQLLT VPSNNATFNK TMSEQQLAFA
460 470 480 490 500
KVRAVEHDRY VVVAGTTGIS AVIAPDGGEL IRTDFFQPAY LDSQVRLKTR
510 520 530 540 550
LTPATRWGPI LQWILVGAAA AVVLVAMRQN GWFPRPRRSE PKGENDDSDA
560 570 580 590 600
PPGRSEASGP PALSESDDEL IQPEQGGRHS SGFGRHRATS RSYMTTGQPA
610 620 630 640 650
PPAPGNRPSQ RVLVIIPTFN ERENLPVIHR RLTQACPAVH VLVVDDSSPD
660 670 680 690 700
GTGQLADELA QADPGRTHVM HRTAKNGLGA AYLAGFAWGL SREYSVLVEM
710 720 730 740 750
DADGSHAPEQ LQRLLDAVDA GADLAIGSRY VAGGTVRNWP WRRLVLSKTA
760 770 780 790 800
NTYSRLALGI GIHDITAGYR AYRREALEAI DLDGVDSKGY CFQIDLTWRT
810 820 830 840 850
VSNGFVVTEV PITFTERELG VSKMSGSNIR EALVKVARWG IEGRLSRSDH
860 870
ARARPDIARP GAGGSRVSRA DVTE
Length:874
Mass (Da):93,824
Last modified:September 16, 2015 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE00EADD2EC3238B4
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AM408590 Genomic DNA Translation: CAL72058.1

NCBI Reference Sequences

More...
RefSeqi
WP_003902238.1, NC_008769.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAL72058; CAL72058; BCG_2070c

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mbb:BCG_2070c

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM408590 Genomic DNA Translation: CAL72058.1
RefSeqiWP_003902238.1, NC_008769.1

3D structure databases

SMRiA0A0H3M5A8
ModBaseiSearch...

Genome annotation databases

EnsemblBacteriaiCAL72058; CAL72058; BCG_2070c
KEGGimbb:BCG_2070c

Phylogenomic databases

KOiK03820
OMAiADEMPND

Enzyme and pathway databases

UniPathwayiUPA00666
BioCyciMBOV410289:G1G1S-2230-MONOMER

Family and domain databases

CDDicd07571 ALP_N-acyl_transferase, 1 hit
cd06442 DPM1_like, 1 hit
Gene3Di3.60.110.10, 1 hit
3.90.550.10, 1 hit
HAMAPiMF_01148 Lnt, 1 hit
InterProiView protein in InterPro
IPR004563 Apolipo_AcylTrfase
IPR003010 C-N_Hydrolase
IPR036526 C-N_Hydrolase_sf
IPR039528 DPM1-like
IPR001173 Glyco_trans_2-like
IPR029044 Nucleotide-diphossugar_trans
PANTHERiPTHR43398 PTHR43398, 1 hit
PfamiView protein in Pfam
PF00795 CN_hydrolase, 1 hit
PF00535 Glycos_transf_2, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit
SSF56317 SSF56317, 1 hit
TIGRFAMsiTIGR00546 lnt, 1 hit
PROSITEiView protein in PROSITE
PS50263 CN_HYDROLASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPPMNT_MYCBP
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A0A0H3M5A8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 11, 2015
Last sequence update: September 16, 2015
Last modified: May 8, 2019
This is version 19 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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