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Protein

Homoserine O-acetyltransferase

Gene

metAA

Organism
Bacillus cereus (strain ATCC 10987 / NRS 248)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in which the acetyl group of acetyl-CoA is initially transferred to the enzyme to form an acetyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-acetylhomoserine. Cannot use succinyl-CoA as the acyl donor.1 Publication

Catalytic activityi

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

Kineticsi

kcat is 58.6 min(-1).1 Publication
  1. KM=185 µM for acetyl-CoA1 Publication
  2. KM=214 µM for homoserine1 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 annotation1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Homoserine O-acetyltransferase (metAA)
    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)DescriptionActionsGraphical viewLength
    Sitei111Important for acyl-CoA specificityUniRule annotation1
    Active sitei142Acyl-thioester intermediateUniRule annotation2 Publications1
    Binding sitei163SubstrateUniRule annotationCombined sources1 Publication1
    Binding sitei192SubstrateUniRule annotationCombined sources1 Publication1
    Sitei192Important for substrate specificityUniRule annotation1
    Active sitei235Proton acceptorUniRule annotation2 Publications1
    Active sitei237UniRule annotation2 Publications1
    Binding sitei249SubstrateUniRule annotationCombined sources1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionAcyltransferase, Transferase
    Biological processAmino-acid biosynthesis, Methionine biosynthesis

    Enzyme and pathway databases

    BRENDAi2.3.1.46. 648.
    UniPathwayiUPA00051; UER00074.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Homoserine O-acetyltransferaseUniRule annotationCurated (EC:2.3.1.31UniRule annotation1 Publication)
    Short name:
    HATUniRule annotationCurated
    Alternative name(s):
    Homoserine transacetylase1 PublicationUniRule annotation
    Short name:
    HTA1 PublicationUniRule annotation
    Gene namesi
    Name:metAAUniRule annotation
    Synonyms:metA1 Publication
    Ordered Locus Names:BCE_5534
    OrganismiBacillus cereus (strain ATCC 10987 / NRS 248)
    Taxonomic identifieri222523 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    Proteomesi
    • UP000002527 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotationCurated

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi47K → M: 17-fold increase in Km for acetyl-CoA and 14-fold decrease in catalytic activity. 1 Publication1
    Mutagenesisi47K → R: 7-fold increase in Km for acetyl-CoA. 1 Publication1
    Mutagenesisi111E → G: No activity with acetyl-CoA but catalyzes an acyltransferase reaction using succinyl-CoA and homoserine. 1 Publication1
    Mutagenesisi142C → A or S: Lack of activity. 1 Publication1
    Mutagenesisi163K → M: 13-fold increase in Km for homoserine. 1 Publication1
    Mutagenesisi192S → A: 5-fold increase in Km for homoserine. 1 Publication1
    Mutagenesisi235H → A, N or Q: Lack of activity. 1 Publication1
    Mutagenesisi237E → A: 65-fold decrease in catalytic activity. 1 Publication1
    Mutagenesisi237E → D: 6-fold decrease in catalytic activity. 1 Publication1
    Mutagenesisi237E → Q: 19-fold decrease in catalytic activity. 1 Publication1
    Mutagenesisi249R → M: 64-fold increase in Km for homoserine and 10-fold decrease in catalytic activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001997361 – 301Homoserine O-acetyltransferaseAdd BLAST301

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1301
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi36 – 41Combined sources6
    Helixi47 – 58Combined sources12
    Beta strandi61 – 63Combined sources3
    Beta strandi65 – 70Combined sources6
    Helixi92 – 95Combined sources4
    Beta strandi100 – 105Combined sources6
    Turni109 – 112Combined sources4
    Helixi115 – 117Combined sources3
    Helixi121 – 134Combined sources14
    Beta strandi135 – 141Combined sources7
    Helixi143 – 153Combined sources11
    Beta strandi158 – 172Combined sources15
    Helixi178 – 180Combined sources3
    Beta strandi185 – 196Combined sources12
    Helixi199 – 203Combined sources5
    Beta strandi208 – 214Combined sources7
    Turni215 – 217Combined sources3
    Beta strandi218 – 224Combined sources7
    Helixi225 – 227Combined sources3
    Beta strandi229 – 232Combined sources4
    Helixi242 – 253Combined sources12
    Helixi265 – 267Combined sources3
    Helixi278 – 291Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2GHRX-ray2.40A1-301[»]
    2VDJX-ray2.00A1-301[»]
    ProteinModelPortaliQ72X44.
    SMRiQ72X44.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ72X44.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MetA family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000115049.
    KOiK00651.
    OMAiCWAAHAA.

    Family and domain databases

    CDDicd03131. GATase1_HTS. 1 hit.
    Gene3Di3.40.50.880. 1 hit.
    HAMAPiMF_00295. MetA_acyltransf. 1 hit.
    InterProiView protein in InterPro
    IPR029062. Class_I_gatase-like.
    IPR005697. HST_MetA.
    IPR033752. MetA_family.
    PANTHERiPTHR20919. PTHR20919. 1 hit.
    PTHR20919:SF1. PTHR20919:SF1. 1 hit.
    PfamiView protein in Pfam
    PF04204. HTS. 1 hit.
    PIRSFiPIRSF000450. H_ser_succinyltr. 1 hit.
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR01001. metA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q72X44-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPIIIDKDLP ARKVLQEENI FVMTKERAET QDIRALKIAI LNLMPTKQET
    60 70 80 90 100
    EAQLLRLIGN TPLQLDVHLL HMESHLSRNV AQEHLTSFYK TFRDIENEKF
    110 120 130 140 150
    DGLIITGAPV ETLSFEEVDY WEELKRIMEY SKTNVTSTLH ICWGAQAGLY
    160 170 180 190 200
    HHYGVQKYPL KEKMFGVFEH EVREQHVKLL QGFDELFFAP HSRHTEVRES
    210 220 230 240 250
    DIREVKELTL LANSEEAGVH LVIGQEGRQV FALGHSEYSC DTLKQEYERD
    260 270 280 290 300
    RDKGLNIDVP KNYFKHDNPN EKPLVRWRSH GNLLFSNWLN YYVYQETPYV

    L
    Length:301
    Mass (Da):35,340
    Last modified:July 5, 2004 - v1
    Checksum:i6476C52969F5067D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE017194 Genomic DNA. Translation: AAS44434.1.
    RefSeqiWP_001121522.1. NC_003909.8.

    Genome annotation databases

    EnsemblBacteriaiAAS44434; AAS44434; BCE_5534.
    KEGGibca:BCE_5534.

    Similar proteinsi

    Entry informationi

    Entry nameiMETAA_BACC1
    AccessioniPrimary (citable) accession number: Q72X44
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: July 5, 2004
    Last modified: August 30, 2017
    This is version 91 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families