AHP1_YEAST
ID AHP1_YEAST Reviewed; 176 AA.
AC P38013; D6VYA9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Peroxiredoxin AHP1 {ECO:0000305};
DE Short=Prx;
DE EC=1.11.1.24 {ECO:0000269|PubMed:10391912, ECO:0000269|PubMed:9888818};
DE AltName: Full=Alkyl hydroperoxide reductase {ECO:0000303|PubMed:9988687};
DE Short=AHPC1;
DE AltName: Full=Cytoplasmic thiol peroxidase 3 {ECO:0000303|PubMed:10681558};
DE Short=cTPx 3 {ECO:0000303|PubMed:10681558};
DE AltName: Full=Thiol-specific antioxidant II {ECO:0000303|PubMed:10681558};
DE Short=TSA II {ECO:0000303|PubMed:10681558};
DE AltName: Full=Thioredoxin peroxidase type II {ECO:0000303|PubMed:9888818};
DE Short=TPx type II;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin AHP1 {ECO:0000305};
GN Name=AHP1 {ECO:0000303|PubMed:9988687}; OrderedLocusNames=YLR109W;
GN ORFNames=L2916, L9354.5;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=9090053;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<241::aid-yea61>3.0.co;2-#;
RA Verhasselt P., Volckaert G.;
RT "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-
RT Arg3 and 23 new open reading frames, among which several homologies to
RT proteins involved in cell division control and to mammalian growth factors
RT and other animal proteins are found.";
RL Yeast 13:241-250(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 2-8; 16-48; 80-102 AND 114-176, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 8-15; 33-41; 80-102 AND 125-176, AND URMYLATION.
RX PubMed=14555475; DOI=10.1128/ec.2.5.930-936.2003;
RA Goehring A.S., Rivers D.M., Sprague G.F. Jr.;
RT "Attachment of the ubiquitin-related protein Urm1p to the antioxidant
RT protein Ahp1p.";
RL Eukaryot. Cell 2:930-936(2003).
RN [6]
RP PROTEIN SEQUENCE OF 16-41; 49-68; 82-96; 114-123 AND 142-150,
RP POST-TRANSLATIONAL MODIFICATION, DISULFIDE BONDS, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9888818; DOI=10.1021/bi9817818;
RA Jeong J.S., Kwon S.J., Kang S.W., Rhee S.G., Kim K.;
RT "Purification and characterization of a second type thioredoxin peroxidase
RT (type II TPx) from Saccharomyces cerevisiae.";
RL Biochemistry 38:776-783(1999).
RN [7]
RP PARTIAL PROTEIN SEQUENCE OF 33-37; 82-96; 126-139 AND 157-170, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=10391912; DOI=10.1074/jbc.274.28.19714;
RA Verdoucq L., Vignols F., Jacquot J.-P., Chartier Y., Meyer Y.;
RT "In vivo characterization of a thioredoxin H target protein defines a new
RT peroxiredoxin family.";
RL J. Biol. Chem. 274:19714-19722(1999).
RN [8]
RP PROTEIN SEQUENCE OF 82-99.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [9]
RP FUNCTION.
RX PubMed=10635552; DOI=10.1271/bbb.63.1871;
RA Farcasanu I.C., Hirata D., Tsuchiya E., Mizuta K., Miyakawa T.;
RT "Involvement of thioredoxin peroxidase type II (Ahp1p) of Saccharomyces
RT cerevisiae in Mn2+ homeostasis.";
RL Biosci. Biotechnol. Biochem. 63:1871-1881(1999).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9988687; DOI=10.1074/jbc.274.8.4537;
RA Lee J., Spector D., Godon C., Labarre J., Toledano M.B.;
RT "A new antioxidant with alkyl hydroperoxide defense properties in yeast.";
RL J. Biol. Chem. 274:4537-4544(1999).
RN [11]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10681558; DOI=10.1074/jbc.275.8.5723;
RA Park S.G., Cha M.-K., Jeong W., Kim I.-H.;
RT "Distinct physiological functions of thiol peroxidase isoenzymes in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:5723-5732(2000).
RN [12]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-116, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [15]
RP FUNCTION.
RX PubMed=20145245; DOI=10.1074/jbc.m109.090142;
RA Iwai K., Naganuma A., Kuge S.;
RT "Peroxiredoxin Ahp1 acts as a receptor for alkylhydroperoxides to induce
RT disulfide bond formation in the Cad1 transcription factor.";
RL J. Biol. Chem. 285:10597-10604(2010).
RN [16]
RP URMYLATION AT LYS-32, AND MUTAGENESIS OF LYS-32.
RX PubMed=21209336; DOI=10.1073/pnas.1014402108;
RA Van der Veen A.G., Schorpp K., Schlieker C., Buti L., Damon J.R.,
RA Spooner E., Ploegh H.L., Jentsch S.;
RT "Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed
RT protein modifier.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1763-1770(2011).
RN [17]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48 AND LYS-113, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [18]
RP 3D-STRUCTURE MODELING, AND STRUCTURE BY NMR.
RX PubMed=14640681; DOI=10.1021/bi035551r;
RA Trivelli X., Krimm I., Ebel C., Verdoucq L., Prouzet-Mauleon V.,
RA Chartier Y., Tsan P., Lauquin G., Meyer Y., Lancelin J.-M.;
RT "Characterization of the yeast peroxiredoxin Ahp1 in its reduced active and
RT overoxidized inactive forms using NMR.";
RL Biochemistry 42:14139-14149(2003).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH TRX2, ACTIVE SITE,
RP DISULFIDE BOND, AND SUBUNIT.
RX PubMed=22474296; DOI=10.1074/jbc.m112.357368;
RA Lian F.M., Yu J., Ma X.X., Yu X.J., Chen Y., Zhou C.Z.;
RT "Structural snapshots of yeast alkyl hydroperoxide reductase Ahp1
RT peroxiredoxin reveal a novel two-cysteine mechanism of electron transfer to
RT eliminate reactive oxygen species.";
RL J. Biol. Chem. 287:17077-17087(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RA Liu M., Wang F., Qiu R., Wu T., Gu S., Tang R., Ji C.;
RT "Crystal structure of Ahp1 from Saccharomyces cerevisiae in reduced form.";
RL Submitted (SEP-2012) to the PDB data bank.
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND DISULFIDE BONDS.
RA Schultz L., Genu V., Breyer C.A., dos Santos V.F., Guimaraes B.G.,
RA de Oliveira M.A., Netto L.E.S.;
RT "Crystal structure of Ahp1 from Saccharomyces cerevisiae. Investigating the
RT electron transfers.";
RL Submitted (FEB-2014) to the PDB data bank.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. Preferentially eliminates organic peroxides rather
CC than hydrogen peroxide (PubMed:10391912, PubMed:9988687,
CC PubMed:10681558). Relays alkyl hydroperoxides as a signal to the
CC transcription factor CAD1/YAP2 by inducing the formation of
CC intramolecular disulfide bonds in CAD1, which causes its nuclear
CC accumulation and activation (PubMed:20145245). Involved in cellular
CC Mn(2+) homeostasis (PubMed:10635552). {ECO:0000269|PubMed:10391912,
CC ECO:0000269|PubMed:10635552, ECO:0000269|PubMed:10681558,
CC ECO:0000269|PubMed:20145245, ECO:0000269|PubMed:9988687}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000269|PubMed:10391912, ECO:0000269|PubMed:9888818};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 uM for H(2)O(2) {ECO:0000269|PubMed:9888818};
CC KM=14 uM for H(2)O(2) {ECO:0000269|PubMed:10391912};
CC KM=8 uM for cumene hydroperoxide {ECO:0000269|PubMed:9888818};
CC KM=45 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:9888818};
CC KM=76.9 uM for tert-butyl hydroperoxide
CC {ECO:0000269|PubMed:22474296};
CC KM=3 uM for TRX1 {ECO:0000269|PubMed:9888818};
CC KM=2 uM for TRX2 {ECO:0000269|PubMed:9888818};
CC KM=1.3 uM for TRX2 {ECO:0000269|PubMed:22474296};
CC Vmax=20 umol/min/mg enzyme for H(2)O(2) {ECO:0000269|PubMed:9888818};
CC Vmax=14 umol/min/mg enzyme for cumene hydroperoxide
CC {ECO:0000269|PubMed:9888818};
CC Vmax=17 umol/min/mg enzyme for tert-butyl hydroperoxide
CC {ECO:0000269|PubMed:9888818};
CC Vmax=17 umol/min/mg enzyme for TRX1 {ECO:0000269|PubMed:9888818};
CC Vmax=16 umol/min/mg enzyme for TRX2 {ECO:0000269|PubMed:9888818};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:9888818};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
CC {ECO:0000269|PubMed:10391912, ECO:0000269|PubMed:22474296,
CC ECO:0000269|PubMed:9888818, ECO:0000269|PubMed:9988687}.
CC -!- INTERACTION:
CC P38013; P34230: PXA2; NbExp=2; IntAct=EBI-2382, EBI-2464632;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10681558}.
CC -!- INDUCTION: By H(2)O(2). {ECO:0000269|PubMed:10681558}.
CC -!- PTM: Conjugated to URM1, a ubiquitin-like protein.
CC {ECO:0000269|PubMed:14555475, ECO:0000269|PubMed:21209336}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC Prx, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000305|PubMed:22474296}.
CC -!- MISCELLANEOUS: Present with 16228 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Biochemical and mutational analysis assigned Cys-120 as the
CC resolving cysteine (C(R)) (PubMed:9888818). However, crystal structures
CC showed that Cys-120 is deeply buried within the protein and revealed
CC formation of a disulfide bond between the peroxidatic cysteine Cys-62
CC and the therefore more likely C(R) Cys-31 (PubMed:22474296, Ref.21).
CC {ECO:0000305|PubMed:22474296, ECO:0000305|PubMed:9888818,
CC ECO:0000305|Ref.21}.
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DR EMBL; X89514; CAA61687.1; -; Genomic_DNA.
DR EMBL; Z73281; CAA97676.1; -; Genomic_DNA.
DR EMBL; U53878; AAB67554.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09425.1; -; Genomic_DNA.
DR PIR; S64946; S64946.
DR RefSeq; NP_013210.1; NM_001181996.1.
DR PDB; 4DSQ; X-ray; 2.40 A; A/B/C/D=1-176.
DR PDB; 4DSR; X-ray; 2.91 A; A/B/C/D=1-176.
DR PDB; 4DSS; X-ray; 2.10 A; A=1-176.
DR PDB; 4H86; X-ray; 2.00 A; A=1-176.
DR PDB; 4OWY; X-ray; 2.20 A; A/B/C/D=1-176.
DR PDB; 7BVV; X-ray; 2.12 A; A=1-176.
DR PDBsum; 4DSQ; -.
DR PDBsum; 4DSR; -.
DR PDBsum; 4DSS; -.
DR PDBsum; 4H86; -.
DR PDBsum; 4OWY; -.
DR PDBsum; 7BVV; -.
DR AlphaFoldDB; P38013; -.
DR BMRB; P38013; -.
DR SMR; P38013; -.
DR BioGRID; 31382; 119.
DR DIP; DIP-6375N; -.
DR IntAct; P38013; 15.
DR MINT; P38013; -.
DR STRING; 4932.YLR109W; -.
DR iPTMnet; P38013; -.
DR COMPLUYEAST-2DPAGE; P38013; -.
DR MaxQB; P38013; -.
DR PaxDb; P38013; -.
DR PRIDE; P38013; -.
DR TopDownProteomics; P38013; -.
DR EnsemblFungi; YLR109W_mRNA; YLR109W; YLR109W.
DR GeneID; 850799; -.
DR KEGG; sce:YLR109W; -.
DR SGD; S000004099; AHP1.
DR VEuPathDB; FungiDB:YLR109W; -.
DR eggNOG; KOG0541; Eukaryota.
DR GeneTree; ENSGT00390000018173; -.
DR HOGENOM; CLU_072440_1_1_1; -.
DR InParanoid; P38013; -.
DR OMA; TPSCHAN; -.
DR BioCyc; YEAST:YLR109W-MON; -.
DR PRO; PR:P38013; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P38013; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:SGD.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0010038; P:response to metal ion; IMP:SGD.
DR CDD; cd03013; PRX5_like; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PTHR10430; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antioxidant; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Isopeptide bond; Oxidoreductase;
KW Peroxidase; Phosphoprotein; Redox-active center; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..176
FT /note="Peroxiredoxin AHP1"
FT /id="PRO_0000056610"
FT DOMAIN 9..176
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 62
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000305|PubMed:22474296"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT DISULFID 31
FT /note="Interchain (with C-31 in TRX2); transient"
FT /evidence="ECO:0000269|PubMed:22474296"
FT DISULFID 31
FT /note="Interchain (with C-62); in linked form"
FT /evidence="ECO:0000269|PubMed:22474296,
FT ECO:0007744|PDB:4DSQ, ECO:0007744|PDB:4OWY"
FT DISULFID 62
FT /note="Interchain (with C-31); in linked form"
FT /evidence="ECO:0000269|PubMed:22474296,
FT ECO:0007744|PDB:4DSQ, ECO:0007744|PDB:4OWY"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in URM1)"
FT /evidence="ECO:0000305|PubMed:21209336"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 31
FT /note="C->S: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:22474296"
FT MUTAGEN 32
FT /note="K->R: Prevents urmylation of AHP1."
FT /evidence="ECO:0000269|PubMed:21209336"
FT MUTAGEN 62
FT /note="C->S: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:22474296"
FT MUTAGEN 120
FT /note="C->S: No effect on tert-butyl hydroperoxide
FT consumption."
FT /evidence="ECO:0000269|PubMed:22474296"
FT CONFLICT 21
FT /note="I -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="S -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="I -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:4H86"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:4H86"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:4H86"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:4OWY"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:4H86"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:4H86"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:4H86"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:4H86"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:4H86"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:4H86"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:4H86"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:4H86"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:4H86"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:4H86"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:4H86"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:4H86"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:4H86"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:4H86"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:4H86"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:4H86"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:4H86"
SQ SEQUENCE 176 AA; 19115 MW; 11B730781306A015 CRC64;
MSDLVNKKFP AGDYKFQYIA ISQSDADSES CKMPQTVEWS KLISENKKVI ITGAPAAFSP
TCTVSHIPGY INYLDELVKE KEVDQVIVVT VDNPFANQAW AKSLGVKDTT HIKFASDPGC
AFTKSIGFEL AVGDGVYWSG RWAMVVENGI VTYAAKETNP GTDVTVSSVE SVLAHL
