AMPL_BOVIN
ID AMPL_BOVIN Reviewed; 519 AA.
AC P00727; Q2HJH5; Q2PC24;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Cytosol aminopeptidase {ECO:0000305};
DE EC=3.4.11.1 {ECO:0000269|PubMed:14583094};
DE AltName: Full=Cysteinylglycine-S-conjugate dipeptidase {ECO:0000305|PubMed:14583094};
DE EC=3.4.13.23 {ECO:0000269|PubMed:14583094};
DE AltName: Full=Leucine aminopeptidase 3 {ECO:0000250|UniProtKB:P28838};
DE Short=LAP-3;
DE AltName: Full=Leucyl aminopeptidase {ECO:0000303|PubMed:14583094};
DE Short=LAP {ECO:0000303|PubMed:14583094};
DE AltName: Full=Peptidase S {ECO:0000250|UniProtKB:P28838};
DE AltName: Full=Proline aminopeptidase {ECO:0000250|UniProtKB:P28839};
DE EC=3.4.11.5 {ECO:0000250|UniProtKB:P28839};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000250|UniProtKB:P28838};
GN Name=LAP3 {ECO:0000250|UniProtKB:P28838};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=8369298; DOI=10.1021/bi00087a006;
RA Wallner B.P., Hession C., Tizard R., Frey A.Z., Zuliani A., Mura C.,
RA Jahngen-Hodge J., Taylor A.;
RT "Isolation of bovine kidney leucine aminopeptidase cDNA: comparison with
RT the lens enzyme and tissue-specific expression of two mRNAs.";
RL Biochemistry 32:9296-9301(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-519 (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE (ISOFORM 3), AND CLEAVAGE OF INITIATOR METHIONINE (ISOFORM
RP 3).
RC TISSUE=Lens;
RX PubMed=7085616; DOI=10.1016/s0021-9258(18)34539-3;
RA Cuypers H.T., van Loon-Klaassen L.A.H., Vree Egberts W.T.M., de Jong W.W.,
RA Bloemendal H.;
RT "The primary structure of leucine aminopeptidase from bovine eye lens.";
RL J. Biol. Chem. 257:7077-7085(1982).
RN [5]
RP PROTEIN SEQUENCE (ISOFORM 3), AND CLEAVAGE OF INITIATOR METHIONINE (ISOFORM
RP 3).
RX PubMed=7085617; DOI=10.1016/s0021-9258(18)34540-x;
RA Cuypers H.T., van Loon-Klaassen L.A.H., Vree Egberts W.T.M., de Jong W.W.,
RA Bloemendal H.;
RT "Sulfhydryl content of bovine eye lens leucine aminopeptidase.
RT Determination of the reactivity of the sulfhydryl groups of the zinc
RT metalloenzyme, of the enzyme activated by Mg2+, Mn2+, and Co2+, and of the
RT metal-free apoenzyme.";
RL J. Biol. Chem. 257:7086-7091(1982).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 431-478.
RC STRAIN=Holstein;
RA Seroussi E.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=14583094; DOI=10.1042/bj20031336;
RA Cappiello M., Lazzarotti A., Buono F., Scaloni A., D'Ambrosio C.,
RA Amodeo P., Mendez B.L., Pelosi P., Del Corso A., Mura U.;
RT "New role for leucyl aminopeptidase in glutathione turnover.";
RL Biochem. J. 378:35-44(2004).
RN [8] {ECO:0007744|PDB:1LAP}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) (ISOFORM 3) IN COMPLEX WITH ZINC, AND
RP CLEAVAGE OF INITIATOR METHIONINE (ISOFORM 3).
RX PubMed=2395881; DOI=10.1073/pnas.87.17.6878;
RA Burley S.K., David P.R., Taylor A., Lipscomb W.N.;
RT "Molecular structure of leucine aminopeptidase at 2.7-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6878-6882(1990).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) (ISOFORM 3) IN COMPLEX WITH BESTATIN,
RP AND CLEAVAGE OF INITIATOR METHIONINE (ISOFORM 3).
RX PubMed=1548695; DOI=10.1016/0022-2836(92)90580-d;
RA Burley S.K., David P.R., Sweet R.M., Taylor A., Lipscomb W.N.;
RT "Structure determination and refinement of bovine lens leucine
RT aminopeptidase and its complex with bestatin.";
RL J. Mol. Biol. 224:113-140(1992).
RN [10] {ECO:0007744|PDB:1BLL}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 33-519 IN COMPLEX WITH ZINC AND
RP AMASTATIN.
RX PubMed=8357796; DOI=10.1021/bi00084a011;
RA Kim H., Lipscomb W.N.;
RT "X-ray crystallographic determination of the structure of bovine lens
RT leucine aminopeptidase complexed with amastatin: formulation of a catalytic
RT mechanism featuring a gem-diolate transition state.";
RL Biochemistry 32:8465-8478(1993).
RN [11] {ECO:0007744|PDB:1BPM, ECO:0007744|PDB:1BPN}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 33-519 IN COMPLEX WITH MAGNESIUM
RP AND ZINC.
RX PubMed=8506345; DOI=10.1073/pnas.90.11.5006;
RA Kim H., Lipscomb W.N.;
RT "Differentiation and identification of the two catalytic metal binding
RT sites in bovine lens leucine aminopeptidase by x-ray crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5006-5010(1993).
RN [12] {ECO:0007744|PDB:1LAM, ECO:0007744|PDB:1LAN}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) (ISOFORM 3) IN COMPLEX WITH ZINC AND
RP LEUCINE, CLEAVAGE OF INITIATOR METHIONINE (ISOFORM 3), AND ACTIVE SITE.
RX PubMed=7578088; DOI=10.1021/bi00045a021;
RA Straeter N., Lipscomb W.N.;
RT "Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site
RT solvent structure and binding mode of L-leucinal, a gem-diolate transition
RT state analogue, by X-ray crystallography.";
RL Biochemistry 34:14792-14800(1995).
RN [13] {ECO:0007744|PDB:1LCP}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 33-516 IN COMPLEX WITH LEUCINE
RP PHOSPHONIC ACID AND ZINC.
RX PubMed=7619821; DOI=10.1021/bi00028a033;
RA Strater N., Lipscomb W.N.;
RT "Transition state analogue L-leucinephosphonic acid bound to bovine lens
RT leucine aminopeptidase: X-ray structure at 1.65 A resolution in a new
RT crystal form.";
RL Biochemistry 34:9200-9210(1995).
RN [14] {ECO:0007744|PDB:2EWB}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 33-518 IN COMPLEX WITH ZINC AND
RP ZOFENOPRILAT, FUNCTION, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16519517; DOI=10.1021/bi052069v;
RA Cappiello M., Alterio V., Amodeo P., Del Corso A., Scaloni A., Pedone C.,
RA Moschini R., De Donatis G.M., De Simone G., Mura U.;
RT "Metal ion substitution in the catalytic site greatly affects the binding
RT of sulfhydryl-containing compounds to leucyl aminopeptidase.";
RL Biochemistry 45:3226-3234(2006).
RN [15] {ECO:0007744|PDB:2J9A}
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 33-519 IN COMPLEX WITH ZINC AND
RP MICROGININ FR1.
RX PubMed=17157838; DOI=10.1016/j.febslet.2006.11.060;
RA Kraft M., Schleberger C., Weckesser J., Schulz G.E.;
RT "Binding structure of the leucine aminopeptidase inhibitor microginin
RT FR1.";
RL FEBS Lett. 580:6943-6947(2006).
CC -!- FUNCTION: Cytosolic metallopeptidase that catalyzes the removal of
CC unsubstituted N-terminal hydrophobic amino acids from various peptides
CC (PubMed:14583094, PubMed:16519517). The presence of Zn(2+) ions is
CC essential for the peptidase activity, and the association with other
CC cofactors can modulate the substrate spectificity of the enzyme
CC (PubMed:16519517). For instance, in the presence of Mn(2+), it displays
CC a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates
CC (PubMed:16519517). Involved in the metabolism of glutathione and in the
CC degradation of glutathione S-conjugates, which may play a role in the
CC control of the cell redox status (PubMed:14583094).
CC {ECO:0000269|PubMed:14583094, ECO:0000269|PubMed:16519517}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000269|PubMed:14583094};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted
CC L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103;
CC EC=3.4.13.23; Evidence={ECO:0000269|PubMed:14583094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445;
CC Evidence={ECO:0000305|PubMed:14583094};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine;
CC Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:61694;
CC Evidence={ECO:0000269|PubMed:14583094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784;
CC Evidence={ECO:0000305|PubMed:14583094};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-
CC cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:145802, ChEBI:CHEBI:145803;
CC Evidence={ECO:0000250|UniProtKB:Q68FS4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569;
CC Evidence={ECO:0000250|UniProtKB:Q68FS4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000250|UniProtKB:P28839};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16519517};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16519517};
CC Note=Binds two metal ions per subunit. Two metal binding sites with
CC different affinities are located in the enzyme active site and can be
CC occupied in vitro by different metals: site 1 is occupied by Zn(2+),
CC Mn(2+), Mg(2+) or Co(2+), while the tight binding site 2 can be
CC occupied by only Zn(2+) or Co(2+) (PubMed:16519517). One Zn(2+) ion is
CC tightly bound to site 2 and essential for enzyme activity in vivo,
CC while site 1 can be occupied by different metals to give different
CC enzymatic activities (PubMed:16519517). Mn(2+) is required for Cys-Gly
CC hydrolysis activity (PubMed:16519517). A third metal binding site may
CC serve a structural role, possibly stabilizing part of the interface
CC between the N-terminal and the catalytic domain (PubMed:7619821).
CC {ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:7619821,
CC ECO:0000303|PubMed:16519517};
CC -!- ACTIVITY REGULATION: Zofenoprilat inhibits Cys-Gly hydrolysis activity.
CC {ECO:0000269|PubMed:16519517}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.42 mM for Cys-Gly (at pH 6.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14583094};
CC KM=2.3 mM for Leu-Gly (at pH 6.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14583094};
CC KM=2.8 mM for Met-Gly (at pH 6.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14583094};
CC KM=0.57 mM for Cys-Gly (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14583094};
CC KM=2.5 mM for Leu-Gly (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14583094};
CC KM=1.5 mM for Met-Gly (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14583094};
CC KM=5.2 mM for Ser-Gly (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14583094};
CC KM=0.59 mM for Cys-Gly (at pH 8.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14583094};
CC KM=1.5 mM for Leu-Gly (at pH 8.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14583094};
CC KM=1.3 mM for Met-Gly (at pH 8.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14583094};
CC KM=5.0 mM for Ser-Gly (at pH 8.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14583094};
CC Note=kcat is 3400 min(-1) for Cys-Gly hydrolysis activity (at pH 6.9
CC and 25 degrees Celsius). kcat is 11500 min(-1) for Leu-Gly hydrolysis
CC activity (at pH 6.9 and 25 degrees Celsius). kcat is 8150 min(-1) for
CC Met-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius)
CC (PubMed:14583094). kcat is 6000 min(-1) for Cys-Gly hydrolysis
CC activity (at pH 7.4 and 25 degrees Celsius). kcat is 24000 min(-1)
CC for Leu-Gly hydrolysis activity (at pH 7.4 and 25 degrees Celsius).
CC kcat is 28100 min(-1) for Met-Gly hydrolysis activity (at pH 7.4 and
CC 25 degrees Celsius). kcat is 1000 min(-1) for Ser-Gly hydrolysis
CC activity (at pH 7.4 and 25 degrees Celsius) (PubMed:14583094). kcat
CC is 7100 min(-1) for Cys-Gly hydrolysis activity (at pH 8.3 and 25
CC degrees Celsius). kcat is 40500 min(-1) for Leu-Gly hydrolysis
CC activity (at pH 8.3 and 25 degrees Celsius). kcat is 59300 min(-1)
CC for Met-Gly hydrolysis activity (at pH 8.3 and 25 degrees Celsius).
CC kcat is 2500 min(-1) for Ser-Gly hydrolysis activity (at pH 8.3 and
CC 25 degrees Celsius) (PubMed:14583094). {ECO:0000269|PubMed:14583094};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:14583094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68FS4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=1;
CC IsoId=P00727-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P00727-2; Sequence=VSP_022634;
CC Name=3;
CC IsoId=P00727-3; Sequence=VSP_058150;
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB28170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S65367; AAB28170.1; ALT_INIT; mRNA.
DR EMBL; BC105385; AAI05386.1; -; mRNA.
DR EMBL; AJ871963; CAI44744.1; -; Genomic_DNA.
DR PIR; A54338; APBOL.
DR RefSeq; NP_776523.2; NM_174098.3. [P00727-1]
DR PDB; 1BLL; X-ray; 2.40 A; E=33-519.
DR PDB; 1BPM; X-ray; 2.90 A; A=33-519.
DR PDB; 1BPN; X-ray; 2.90 A; A=33-519.
DR PDB; 1LAM; X-ray; 1.60 A; A=33-516.
DR PDB; 1LAN; X-ray; 1.90 A; A=33-516.
DR PDB; 1LAP; X-ray; 2.70 A; A=33-519.
DR PDB; 1LCP; X-ray; 1.65 A; A/B=33-516.
DR PDB; 2EWB; X-ray; 1.85 A; A=33-518.
DR PDB; 2J9A; X-ray; 1.73 A; A=33-519.
DR PDBsum; 1BLL; -.
DR PDBsum; 1BPM; -.
DR PDBsum; 1BPN; -.
DR PDBsum; 1LAM; -.
DR PDBsum; 1LAN; -.
DR PDBsum; 1LAP; -.
DR PDBsum; 1LCP; -.
DR PDBsum; 2EWB; -.
DR PDBsum; 2J9A; -.
DR AlphaFoldDB; P00727; -.
DR SMR; P00727; -.
DR STRING; 9913.ENSBTAP00000007860; -.
DR BindingDB; P00727; -.
DR ChEMBL; CHEMBL1671610; -.
DR DrugCentral; P00727; -.
DR MEROPS; M17.001; -.
DR PaxDb; P00727; -.
DR PeptideAtlas; P00727; -.
DR PRIDE; P00727; -.
DR Ensembl; ENSBTAT00000007860; ENSBTAP00000007860; ENSBTAG00000005989. [P00727-1]
DR GeneID; 781648; -.
DR KEGG; bta:781648; -.
DR CTD; 51056; -.
DR VEuPathDB; HostDB:ENSBTAG00000005989; -.
DR eggNOG; KOG2597; Eukaryota.
DR GeneTree; ENSGT00530000063255; -.
DR InParanoid; P00727; -.
DR OMA; MKNTGPR; -.
DR OrthoDB; 562530at2759; -.
DR TreeFam; TF314954; -.
DR BRENDA; 3.4.11.1; 908.
DR SABIO-RK; P00727; -.
DR EvolutionaryTrace; P00727; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000005989; Expressed in caput epididymis and 102 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:RHEA.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; ISS:AgBase.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Aminopeptidase; Cobalt;
KW Cytoplasm; Dipeptidase; Direct protein sequencing; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Phosphoprotein; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..519
FT /note="Cytosol aminopeptidase"
FT /id="PRO_0000165824"
FT ACT_SITE 294
FT /evidence="ECO:0000269|PubMed:7578088"
FT ACT_SITE 368
FT /evidence="ECO:0000269|PubMed:7578088"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000305|PubMed:7619821,
FT ECO:0007744|PDB:1LCP"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000305|PubMed:7619821,
FT ECO:0007744|PDB:1LCP"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000305|PubMed:7619821,
FT ECO:0007744|PDB:1LCP"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:7578088,
FT ECO:0000269|PubMed:7619821, ECO:0007744|PDB:1LAN,
FT ECO:0007744|PDB:1LCP"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16519517,
FT ECO:0000269|PubMed:17157838, ECO:0007744|PDB:2EWB,
FT ECO:0007744|PDB:2J9A"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:8506345,
FT ECO:0007744|PDB:1BPM"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:7578088,
FT ECO:0000269|PubMed:7619821, ECO:0007744|PDB:1LAN,
FT ECO:0007744|PDB:1LCP"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16519517,
FT ECO:0000269|PubMed:17157838, ECO:0000269|PubMed:8506345,
FT ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16519517,
FT ECO:0000269|PubMed:17157838, ECO:0007744|PDB:2EWB,
FT ECO:0007744|PDB:2J9A"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:7619821,
FT ECO:0007744|PDB:1LCP"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:7578088,
FT ECO:0000269|PubMed:7619821, ECO:0007744|PDB:1LAN,
FT ECO:0007744|PDB:1LCP"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000305|PubMed:7619821,
FT ECO:0007744|PDB:1LCP"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:7578088,
FT ECO:0007744|PDB:1LAN"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16519517,
FT ECO:0000269|PubMed:17157838, ECO:0007744|PDB:2EWB,
FT ECO:0007744|PDB:2J9A"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:8506345,
FT ECO:0007744|PDB:1BPM"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:7619821,
FT ECO:0007744|PDB:1LCP"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16519517,
FT ECO:0000269|PubMed:17157838, ECO:0000269|PubMed:8506345,
FT ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:8506345,
FT ECO:0007744|PDB:1BPM"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16519517,
FT ECO:0000269|PubMed:17157838, ECO:0000269|PubMed:8506345,
FT ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16519517,
FT ECO:0000269|PubMed:17157838, ECO:0000269|PubMed:8506345,
FT ECO:0007744|PDB:1BPM, ECO:0007744|PDB:2EWB,
FT ECO:0007744|PDB:2J9A"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FS4"
FT MOD_RES 45
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FS4"
FT MOD_RES 61
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28838"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28838"
FT MOD_RES 455
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 455
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 476
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 489
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 489
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_058150"
FT VAR_SEQ 11..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8369298"
FT /id="VSP_022634"
FT CONFLICT 77
FT /note="P -> S (in Ref. 2; AAB28170)"
FT /evidence="ECO:0000305"
FT CONFLICT 414..415
FT /note="LW -> M (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 506..513
FT /note="Missing (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1BPM"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:1LAM"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:1LAM"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 116..134
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 183..204
FT /evidence="ECO:0007829|PDB:1LAM"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 212..226
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 307..321
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 325..337
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:1LAM"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:1BPN"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 394..400
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 412..425
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 436..443
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 446..453
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 460..469
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 475..481
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:1LAM"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:1LAM"
FT HELIX 504..515
FT /evidence="ECO:0007829|PDB:1LAM"
FT INIT_MET P00727-3:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1548695,
FT ECO:0000269|PubMed:2395881, ECO:0000269|PubMed:7085616,
FT ECO:0000269|PubMed:7085617, ECO:0000269|PubMed:7578088"
SQ SEQUENCE 519 AA; 56289 MW; CDA6AED4D937F624 CRC64;
MFLLPLPAAA RVAVRHLSVK RLWAPGPAAA DMTKGLVLGI YSKEKEEDEP QFTSAGENFN
KLVSGKLREI LNISGPPLKA GKTRTFYGLH EDFPSVVVVG LGKKTAGIDE QENWHEGKEN
IRAAVAAGCR QIQDLEIPSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKRK VVVSAKLHGS
EDQEAWQRGV LFASGQNLAR RLMETPANEM TPTKFAEIVE ENLKSASIKT DVFIRPKSWI
EEQEMGSFLS VAKGSEEPPV FLEIHYKGSP NASEPPLVFV GKGITFDSGG ISIKAAANMD
LMRADMGGAA TICSAIVSAA KLDLPINIVG LAPLCENMPS GKANKPGDVV RARNGKTIQV
DNTDAEGRLI LADALCYAHT FNPKVIINAA TLTGAMDIAL GSGATGVFTN SSWLWNKLFE
ASIETGDRVW RMPLFEHYTR QVIDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL
DIAGVMTNKD EVPYLRKGMA GRPTRTLIEF LFRFSQDSA
