HAT1_MAIZE
ID HAT1_MAIZE Reviewed; 468 AA.
AC Q8LPU4; O49994;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:O14929};
DE AltName: Full=Histone acetyltransferase HAT B;
DE AltName: Full=Histone acetyltransferase HAT-B-p50;
GN Name=HAT1; Synonyms=HAC106, HATB1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH P45,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Cuzco 251;
RX PubMed=10536152; DOI=10.1093/nar/27.22.4427;
RA Lusser A., Eberharter A., Loidl A., Goralik-Schramel M., Horngacher M.,
RA Hass H., Loidl P.;
RT "Analysis of the histone acetyltransferase B complex of maize embryos.";
RL Nucleic Acids Res. 27:4427-4435(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73;
RA Chandler V.L., Kaeppler S.M., Kaeppler H.F., Cone K.C.;
RT "Sequences from the plant chromatin consortium.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8635608; DOI=10.1016/0014-5793(96)00401-2;
RA Eberharter A., Lechner T., Goralik-Schramel M., Loidl P.;
RT "Purification and characterization of the cytoplasmic histone
RT acetyltransferase B of maize embryos.";
RL FEBS Lett. 386:75-81(1996).
RN [4]
RP SUBSTRATE SPECIFICITY.
RX PubMed=9468289; DOI=10.1016/s0014-5793(97)01544-5;
RA Koelle D., Sarg B., Lindner H., Loidl P.;
RT "Substrate and sequential site specificity of cytoplasmic histone
RT acetyltransferases of maize and rat liver.";
RL FEBS Lett. 421:109-114(1998).
CC -!- FUNCTION: Acetylates newly synthesized histones during DNA replication.
CC Highly specific in vitro for the non-acetylated H4 which is acetylated
CC sequentially at 'Lys-12' and 'Lys-5' into a di-acetylated form.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:O14929};
CC -!- ACTIVITY REGULATION: Inhibited by 5 mM of zinc, copper and iron.
CC Unaffected by low concentrations of detergents and irreversibly
CC inactivated by 2% ethanol, isopropanol or dimethyl sulfoxide.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for core histones {ECO:0000269|PubMed:8635608};
CC KM=9 uM for acetyl-CoA {ECO:0000269|PubMed:8635608};
CC pH dependence:
CC Optimum pH is 8.2-8.5. {ECO:0000269|PubMed:8635608};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:8635608};
CC -!- SUBUNIT: Heteromer of HAT1/p50 and p45 subunits.
CC {ECO:0000269|PubMed:10536152}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10536152}. Cytoplasm
CC {ECO:0000269|PubMed:10536152}.
CC -!- DEVELOPMENTAL STAGE: Found in the dry embryo (at protein level).
CC Maximum level of expression 22 hours after start of seed imbibition.
CC {ECO:0000269|PubMed:10536152}.
CC -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
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DR EMBL; U90274; AAC03423.2; -; mRNA.
DR EMBL; AF171927; AAF06742.1; -; Genomic_DNA.
DR EMBL; AY093417; AAM28228.1; -; mRNA.
DR PIR; T02064; T02064.
DR RefSeq; NP_001105187.1; NM_001111717.1.
DR RefSeq; XP_008651846.1; XM_008653624.1.
DR AlphaFoldDB; Q8LPU4; -.
DR SMR; Q8LPU4; -.
DR STRING; 4577.GRMZM5G851405_P02; -.
DR PaxDb; Q8LPU4; -.
DR PRIDE; Q8LPU4; -.
DR GeneID; 542083; -.
DR KEGG; zma:542083; -.
DR MaizeGDB; 273678; -.
DR eggNOG; KOG2696; Eukaryota.
DR OrthoDB; 708105at2759; -.
DR BRENDA; 2.3.1.48; 6752.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q8LPU4; baseline and differential.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:InterPro.
DR Gene3D; 3.90.360.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR019467; Hat1_N.
DR InterPro; IPR037113; Hat1_N_sf.
DR InterPro; IPR017380; Hist_AcTrfase_B-typ_cat-su.
DR PANTHER; PTHR12046; PTHR12046; 1.
DR Pfam; PF10394; Hat1_N; 1.
DR PIRSF; PIRSF038084; HAT-B_cat; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..468
FT /note="Histone acetyltransferase type B catalytic subunit"
FT /id="PRO_0000232126"
FT ACT_SITE 276
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT BINDING 242..244
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT BINDING 249..255
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT SITE 200
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT CONFLICT 354
FT /note="V -> I (in Ref. 2; AAM28228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 52721 MW; 049F68157ED8443C CRC64;
MALKQKDTDA AATATGTKKR RRVFFSDTDA GVEANECMKV FLVWNPGEVS SVDCTAIQPF
DLNHFFGEDG KIYGYKNLKI NVWISAKSFH GYADVSFDET SDGGKGITDL KPVLQNIFGE
NLVEKEEFLH TFSKECEYIR TAVTNGSAIK HDGSYESDPA VEIVRVELQG AAAFLYSRLV
PLVLLLVEGS TPIDIGEHGW EMLLVVKKAT QEAGSKFELL GFAAVHNFYH YPESIRLRIS
QILVLPPYQG EGHGLGLLEA INYIAQSENI YDVTIESPSD YLQYVRSSID CLRLLMFDPI
KPALGAIVLS LKETNLSKRA QSLRMVPPAD LMETVRQKLK INKKQFLRCW EILVFLSLDS
QDHKSMDNFR ACIYDRMKGE ILGSASGTNR KRLLQMPTSF NKEASFAVYW TQEIEDEDEQ
TVEQQPEDLK TQEQQLNELV DIQIEEIAGV AKNVTSRCKD KMTELVVQ
