PUR9_MOUSE
ID PUR9_MOUSE Reviewed; 592 AA.
AC Q9CWJ9; Q3UTQ3; Q80UH0; Q8BPF0; Q8BQV9; Q9CRI1; Q9CZW9;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Bifunctional purine biosynthesis protein ATIC;
DE AltName: Full=AICAR transformylase/inosine monophosphate cyclohydrolase;
DE Short=ATIC;
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase;
DE EC=2.1.2.3 {ECO:0000269|PubMed:29072452};
DE AltName: Full=5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase;
DE Short=AICAR formyltransferase;
DE AltName: Full=AICAR transformylase;
DE Includes:
DE RecName: Full=IMP cyclohydrolase;
DE EC=3.5.4.10 {ECO:0000250|UniProtKB:P31939};
DE AltName: Full=IMP synthase;
DE AltName: Full=Inosinicase;
GN Name=Atic; Synonyms=Purh;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Corpora quadrigemina, and Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 98-108; 178-194 AND 531-545, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Friebe K., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=29072452; DOI=10.1021/acs.jmedchem.7b01046;
RA Fales K.R., Njoroge F.G., Brooks H.B., Thibodeaux S., Torrado A., Si C.,
RA Toth J.L., Mc Cowan J.R., Roth K.D., Thrasher K.J., Frimpong K., Lee M.R.,
RA Dally R.D., Shepherd T.A., Durham T.B., Margolis B.J., Wu Z., Wang Y.,
RA Atwell S., Wang J., Hui Y.H., Meier T.I., Konicek S.A., Geeganage S.;
RT "Discovery of LSN 3213128, a Potent and Selective Nonclassical Antifolate
RT Aminoimidazole-4-carboxamide Ribonucleotide Formyltransferase (AICARFT)
RT Inhibitor Effective at Tumor Suppression in a Cancer Xenograft Model.";
RL J. Med. Chem. 60:9599-9616(2017).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the last two steps of
CC purine biosynthesis (PubMed:29072452). Acts as a transformylase that
CC incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-
CC phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the
CC intermediate formyl-AICAR (FAICAR) (PubMed:29072452). Also displays
CC cyclohydrolase activity involving the cyclization of FAICAR to IMP. Can
CC use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the
CC formyl donor in this reaction. Also catalyzes the cyclization of FAICAR
CC to IMP. Promotes insulin receptor/INSR autophosphorylation and is
CC involved in INSR internalization (By similarity).
CC {ECO:0000250|UniProtKB:P31939, ECO:0000269|PubMed:29072452}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; EC=2.1.2.3;
CC Evidence={ECO:0000269|PubMed:29072452};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22193;
CC Evidence={ECO:0000269|PubMed:29072452};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=10-formyldihydrofolate + 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D-
CC ribosyl)imidazole-4-carboxamide + 7,8-dihydrofolate;
CC Xref=Rhea:RHEA:59144, ChEBI:CHEBI:57451, ChEBI:CHEBI:57452,
CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475;
CC Evidence={ECO:0000250|UniProtKB:P31939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59145;
CC Evidence={ECO:0000250|UniProtKB:P31939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC Evidence={ECO:0000250|UniProtKB:P31939};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18447;
CC Evidence={ECO:0000250|UniProtKB:P31939};
CC -!- ACTIVITY REGULATION: AMP and XMP inhibit AICAR formyltransferase
CC activity (By similarity). AICAR formyltransferase activity is inhibited
CC by N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5- [(3R)-3-
CC hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide (LSN 3213128), which
CC acts as a tumor suppression in cancer cell lines (PubMed:29072452).
CC {ECO:0000250|UniProtKB:P31939, ECO:0000269|PubMed:29072452}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC step 1/1. {ECO:0000269|PubMed:29072452}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC 1/1. {ECO:0000250|UniProtKB:P31939}.
CC -!- SUBUNIT: Homodimer. Associates with internalized INSR complexes on
CC Golgi/endosomal membranes. Interacts with INSR; ATIC together with
CC PRKAA2/AMPK2 and HACD3/PTPLAD1 is proposed to be part of a signaling
CC network regulating INSR autophosphorylation and endocytosis.
CC {ECO:0000250|UniProtKB:P31939}.
CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC region.
CC -!- MISCELLANEOUS: The de novo purine synthesis pathway includes 10
CC sequential steps, beginning with phosphoribosyl pyrophosphate and
CC ending with inositol monophosphate (IMP), the first purin compound of
CC the pathway. {ECO:0000250|UniProtKB:P31939}.
CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28011.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK010449; BAB26949.3; -; mRNA.
DR EMBL; AK010611; BAB27060.1; -; mRNA.
DR EMBL; AK012074; BAB28011.1; ALT_FRAME; mRNA.
DR EMBL; AK046353; BAC32688.1; -; mRNA.
DR EMBL; AK076091; BAC36175.1; -; mRNA.
DR EMBL; AK139235; BAE23927.1; -; mRNA.
DR EMBL; BC039925; AAH39925.2; -; mRNA.
DR CCDS; CCDS15030.1; -.
DR RefSeq; NP_080471.2; NM_026195.3.
DR AlphaFoldDB; Q9CWJ9; -.
DR SMR; Q9CWJ9; -.
DR BioGRID; 223864; 16.
DR IntAct; Q9CWJ9; 1.
DR STRING; 10090.ENSMUSP00000027384; -.
DR BindingDB; Q9CWJ9; -.
DR ChEMBL; CHEMBL2277; -.
DR iPTMnet; Q9CWJ9; -.
DR PhosphoSitePlus; Q9CWJ9; -.
DR SwissPalm; Q9CWJ9; -.
DR REPRODUCTION-2DPAGE; Q9CWJ9; -.
DR CPTAC; non-CPTAC-3870; -.
DR CPTAC; non-CPTAC-3941; -.
DR EPD; Q9CWJ9; -.
DR jPOST; Q9CWJ9; -.
DR MaxQB; Q9CWJ9; -.
DR PaxDb; Q9CWJ9; -.
DR PeptideAtlas; Q9CWJ9; -.
DR PRIDE; Q9CWJ9; -.
DR ProteomicsDB; 301954; -.
DR Antibodypedia; 4601; 424 antibodies from 36 providers.
DR DNASU; 108147; -.
DR Ensembl; ENSMUST00000027384; ENSMUSP00000027384; ENSMUSG00000026192.
DR GeneID; 108147; -.
DR KEGG; mmu:108147; -.
DR UCSC; uc007bjs.2; mouse.
DR CTD; 471; -.
DR MGI; MGI:1351352; Atic.
DR VEuPathDB; HostDB:ENSMUSG00000026192; -.
DR eggNOG; KOG2555; Eukaryota.
DR GeneTree; ENSGT00390000004553; -.
DR HOGENOM; CLU_016316_3_2_1; -.
DR InParanoid; Q9CWJ9; -.
DR OMA; WRVAKFV; -.
DR OrthoDB; 143470at2759; -.
DR PhylomeDB; Q9CWJ9; -.
DR TreeFam; TF105642; -.
DR Reactome; R-MMU-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR BioGRID-ORCS; 108147; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Atic; mouse.
DR PRO; PR:Q9CWJ9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CWJ9; protein.
DR Bgee; ENSMUSG00000026192; Expressed in manus and 228 other tissues.
DR Genevisible; Q9CWJ9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IMP:MGI.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IMP:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IMP:MGI.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IMP:MGI.
DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; IMP:MGI.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0003360; P:brainstem development; IEA:Ensembl.
DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0046452; P:dihydrofolate metabolic process; ISO:MGI.
DR GO; GO:0006177; P:GMP biosynthetic process; IMP:MGI.
DR GO; GO:0009116; P:nucleoside metabolic process; ISO:MGI.
DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
DR GO; GO:0009259; P:ribonucleotide metabolic process; ISO:MGI.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; ISO:MGI.
DR Gene3D; 1.10.287.440; -; 1.
DR Gene3D; 3.40.140.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_00139; PurH; 1.
DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR InterPro; IPR024050; AICAR_Tfase_insert_dom_sf.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR002695; PurH-like.
DR PANTHER; PTHR11692; PTHR11692; 1.
DR Pfam; PF01808; AICARFT_IMPCHas; 1.
DR Pfam; PF02142; MGS; 1.
DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR SMART; SM00798; AICARFT_IMPCHas; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR TIGRFAMs; TIGR00355; purH; 1.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Hydrolase; Multifunctional enzyme;
KW Purine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..592
FT /note="Bifunctional purine biosynthesis protein ATIC"
FT /id="PRO_0000192157"
FT DOMAIN 1..146
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..198
FT /note="IMP cyclohydrolase"
FT /evidence="ECO:0000250|UniProtKB:P31335"
FT REGION 199..592
FT /note="AICAR formyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P31335"
FT ACT_SITE 137
FT /note="Proton donor/acceptor; for FAICAR cyclization
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT ACT_SITE 267
FT /note="Proton acceptor; for AICAR formyltransferase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 12..14
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 34..37
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 64..67
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 101..102
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 125..126
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 207..208
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 267
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 316
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 339
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 431
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 451
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 452
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P31335"
FT BINDING 541
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 546
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P31335"
FT BINDING 565..566
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:P31335"
FT BINDING 588
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT SITE 266
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT CONFLICT 22
FT /note="R -> K (in Ref. 1; BAB26949)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="A -> T (in Ref. 1; BAE23927)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="L -> S (in Ref. 2; AAH39925)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="Y -> C (in Ref. 1; BAB27060)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 64217 MW; 8C5278040059FB5D CRC64;
MAPSQLALFS VSDKTGLVEF ARSLASLGLS LVASGGTAKA IRDAGLAVRD VSELTGFPEM
LGGRVKTLHP AVHAGILARN IPEDAADMAR LDFNLVRVVV CNLYPFVKTV ASPDVTVEAA
VEQIDIGGVT LLRAAAKNHA RVTVVCEPED YAGVAAEMHG SDSKDTSLET RRHLALKAFT
HTAQYDEAIS DYFRKQYSKG ISQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL
CDALNAWQLV TELRGAVDIP AAASFKHVSP AGAAVGVPLS EDEARVCMVY DLYPTLTPLA
VAYARARGAD RMSSFGDFVA LSDICDVPTA KIISREVSDG IVAPGYEEEA LKILSKKKNG
NYCVLQMDQS YKPDENEVRT LFGLRLSQKR NNGVVDKSLF SNIVTKNKDL PESALRDLIV
ATVAVKYTQS NSVCYAKDGQ VIGIGAGQQS RIHCTRLAGD KANSWWLRHH PRVLSMKFKA
GVKRAEISNA IDQYVTGTIG EGEDLVKWEA LFEEVPELLT EAEKKEWVDK LSGVSVSSDA
FFPFRDNVDR AKRSGVAYIV APSGSTADKV VIEACDELGI VLAHTDLRLF HH
