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UniProtKB - P45131 (METX_HAEIN)

UniProt

P45131 - METX_HAEIN

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Protein

Homoserine O-acetyltransferase

Gene

metX

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

Functioni

Involved in the methionine biosynthesis. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-homoserine to yield O-acetyl-L-homoserine.UniRule annotation1 Publication

Catalytic activityi

Acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine.UniRule annotation1 Publication

Kineticsi

Kcat is 92 (sec-1) for acetyl-CoA and L-homoserin (at 25 degrees Celsius and pH 7.5).

  1. KM=90 µM for propionyl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
  2. KM=130 µM for crotonyl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
  3. KM=130 µM for L-homoserine (at 25 degrees Celsius and pH 7.5)1 Publication
  4. KM=140 µM for acetyl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
  5. KM=210 µM for butyryl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
  6. KM=280 µM for glutaryl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
  7. KM=360 µM for succinyl-CoA (at 25 degrees Celsius and pH 7.5)1 Publication
  8. KM=1400 µM for 4-nitrophenyl acetate (at 25 degrees Celsius and pH 7.5)1 Publication
  9. KM=4700 µM for D-homoserine (at 25 degrees Celsius and pH 7.5)1 Publication

    Pathwayi: L-methionine biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes O-acetyl-L-homoserine from L-homoserine.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Homoserine O-acetyltransferase (metX)
    This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes O-acetyl-L-homoserine from L-homoserine, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei143 – 1431NucleophileUniRule annotation
    Active sitei304 – 3041UniRule annotation
    Active sitei337 – 3371UniRule annotation

    GO - Molecular functioni

    • homoserine O-acetyltransferase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Enzyme and pathway databases

    BRENDAi2.3.1.31. 2529.
    UniPathwayiUPA00051; UER00074.

    Protein family/group databases

    ESTHERihaein-metx. Homoserine_transacetylase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Homoserine O-acetyltransferaseUniRule annotation (EC:2.3.1.31UniRule annotation)
    Alternative name(s):
    Homoserine O-trans-acetylaseUniRule annotation
    Short name:
    HTAUniRule annotation
    Short name:
    Homoserine transacetylaseUniRule annotation
    Gene namesi
    Name:metXUniRule annotation
    Synonyms:met2
    Ordered Locus Names:HI_1263
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus ›
    Proteomesi
    • UP000000579 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 358357Homoserine O-acetyltransferasePRO_0000155719Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation2 Publications

    Protein-protein interaction databases

    STRINGi71421.HI1263.

    Structurei

    Secondary structure

    1
    358
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 129Combined sources
    Beta strandi24 – 3310Combined sources
    Beta strandi42 – 465Combined sources
    Beta strandi58 – 603Combined sources
    Helixi66 – 683Combined sources
    Beta strandi73 – 764Combined sources
    Turni77 – 793Combined sources
    Beta strandi81 – 855Combined sources
    Beta strandi91 – 955Combined sources
    Turni102 – 1043Combined sources
    Beta strandi105 – 1073Combined sources
    Helixi109 – 1113Combined sources
    Helixi117 – 13014Combined sources
    Beta strandi136 – 1427Combined sources
    Helixi144 – 15512Combined sources
    Beta strandi159 – 1679Combined sources
    Helixi174 – 18815Combined sources
    Helixi194 – 1963Combined sources
    Helixi205 – 21915Combined sources
    Helixi222 – 2287Combined sources
    Turni229 – 2313Combined sources
    Helixi245 – 25814Combined sources
    Helixi263 – 27513Combined sources
    Turni278 – 2814Combined sources
    Helixi285 – 2895Combined sources
    Beta strandi294 – 3018Combined sources
    Beta strandi305 – 3073Combined sources
    Helixi309 – 32113Combined sources
    Beta strandi325 – 3317Combined sources
    Helixi336 – 3383Combined sources
    Helixi339 – 3424Combined sources
    Helixi344 – 35613Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B61X-ray1.65A1-358[»]
    ProteinModelPortaliP45131.
    SMRiP45131. Positions 2-358.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45131.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. HTA family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105DWV. Bacteria.
    COG2021. LUCA.
    KOiK00641.
    OMAiGSVGGMN.
    PhylomeDBiP45131.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    HAMAPiMF_00296. Homoser_O_acetyltr. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR008220. Homoserine_AcTrfase.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000443. Homoser_Ac_trans. 1 hit.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    TIGRFAMsiTIGR01392. homoserO_Ac_trn. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P45131-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSVQNVVLFD TQPLTLMLGG KLSHINVAYQ TYGTLNAEKN NAVLICHALT 
            60         70         80         90        100
    GDAEPYFDDG RDGWWQNFMG AGLALDTDRY FFISSNVLGG CKGTTGPSSI 
           110        120        130        140        150
    NPQTGKPYGS QFPNIVVQDI VKVQKALLDH LGISHLKAII GGSFGGMQAN 
           160        170        180        190        200
    QWAIDYPDFM DNIVNLCSSI YFSAEAIGFN HVMRQAVIND PNFNGGDYYE 
           210        220        230        240        250
    GTPPDQGLSI ARMLGMLTYR TDLQLAKAFG RATKSDGSFW GDYFQVESYL 
           260        270        280        290        300
    SYQGKKFLER FDANSYLHLL RALDMYDPSL GYDNVKEALS RIKARYTLVS 
           310        320        330        340        350
    VTTDQLFKPI DLYKSKQLLE QSGVDLHFYE FPSDYGHDAF LVDYDQFEKR 

    IRDGLAGN
    Length:358
    Mass (Da):39,990
    Last modified:January 23, 2007 - v3
    Checksum:i2484D6BEAC761983
    GO

    Mass spectrometryi

    Molecular mass is 39859 Da from positions 2 - 358. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		L42023 Genomic DNA. Translation: AAC22916.1.
    PIRiD64113.
    RefSeqiNP_439418.1. NC_000907.1.
    WP_005694320.1. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC22916; AAC22916; HI_1263.
    GeneIDi950208.
    KEGGihin:HI1263.
    PATRICi20191207. VBIHaeInf48452_1315.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		L42023 Genomic DNA. Translation: AAC22916.1.
    PIRiD64113.
    RefSeqiNP_439418.1. NC_000907.1.
    WP_005694320.1. NC_000907.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B61X-ray1.65A1-358[»]
    ProteinModelPortaliP45131.
    SMRiP45131. Positions 2-358.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi71421.HI1263.

    Protein family/group databases

    ESTHERihaein-metx. Homoserine_transacetylase.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC22916; AAC22916; HI_1263.
    GeneIDi950208.
    KEGGihin:HI1263.
    PATRICi20191207. VBIHaeInf48452_1315.

    Phylogenomic databases

    eggNOGiENOG4105DWV. Bacteria.
    COG2021. LUCA.
    KOiK00641.
    OMAiGSVGGMN.
    PhylomeDBiP45131.

    Enzyme and pathway databases

    UniPathwayiUPA00051; UER00074.
    BRENDAi2.3.1.31. 2529.

    Miscellaneous databases

    EvolutionaryTraceiP45131.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    HAMAPiMF_00296. Homoser_O_acetyltr. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR008220. Homoserine_AcTrfase.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000443. Homoser_Ac_trans. 1 hit.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    TIGRFAMsiTIGR01392. homoserO_Ac_trn. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMETX_HAEIN
    AccessioniPrimary (citable) accession number: P45131
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: September 7, 2016
    This is version 124 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.