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Database: UniProt/SWISS-PROT
Entry: GABT_ECOLI
LinkDB: GABT_ECOLI
Original site: GABT_ECOLI 
ID   GABT_ECOLI              Reviewed;         426 AA.
AC   P22256;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   13-FEB-2019, entry version 165.
DE   RecName: Full=4-aminobutyrate aminotransferase GabT;
DE            EC=2.6.1.19 {ECO:0000269|PubMed:15723541, ECO:0000269|PubMed:30498244};
DE   AltName: Full=5-aminovalerate transaminase {ECO:0000305|PubMed:30498244};
DE            EC=2.6.1.48 {ECO:0000269|PubMed:30498244};
DE   AltName: Full=GABA aminotransferase;
DE            Short=GABA-AT;
DE   AltName: Full=Gamma-amino-N-butyrate transaminase;
DE            Short=GABA transaminase;
DE   AltName: Full=Glutamate:succinic semialdehyde transaminase;
DE   AltName: Full=L-AIBAT;
GN   Name=gabT; OrderedLocusNames=b2662, JW2637;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2254272; DOI=10.1128/jb.172.12.7035-7042.1990;
RA   Bartsch K., von Johnn-Marteville A., Schulz A.;
RT   "Molecular analysis of two genes of the Escherichia coli gab cluster:
RT   nucleotide sequence of the glutamate:succinic semialdehyde
RT   transaminase gene (gabT) and characterization of the succinic
RT   semialdehyde dehydrogenase gene (gabD).";
RL   J. Bacteriol. 172:7035-7042(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA   Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA   Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA   Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA   Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA   Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT   K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT   analysis of its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-30.
RC   STRAIN=K12;
RX   PubMed=2178550;
RA   Schulz A., Taggeselle P., Tripier D., Bartsch K.;
RT   "Stereospecific production of the herbicide phosphinothricin
RT   (glufosinate) by transamination: isolation and characterization of a
RT   phosphinothricin-specific transaminase from Escherichia coli.";
RL   Appl. Environ. Microbiol. 56:1-6(1990).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, AND INDUCTION.
RC   STRAIN=K12;
RX   PubMed=12446648; DOI=10.1128/JB.184.24.6976-6986.2002;
RA   Schneider B.L., Ruback S., Kiupakis A.K., Kasbarian H., Pybus C.,
RA   Reitzer L.;
RT   "The Escherichia coli gabDTPC operon: specific gamma-aminobutyrate
RT   catabolism and nonspecific induction.";
RL   J. Bacteriol. 184:6976-6986(2002).
RN   [7]
RP   INDUCTION.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=14731280; DOI=10.1046/j.1365-2958.2003.03867.x;
RA   Metzner M., Germer J., Hengge R.;
RT   "Multiple stress signal integration in the regulation of the complex
RT   sigma S-dependent csiD-ygaF-gabDTP operon in Escherichia coli.";
RL   Mol. Microbiol. 51:799-811(2004).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=20639325; DOI=10.1128/JB.00308-10;
RA   Kurihara S., Kato K., Asada K., Kumagai H., Suzuki H.;
RT   "A putrescine-inducible pathway comprising PuuE-YneI in which gamma-
RT   aminobutyrate is degraded into succinate in Escherichia coli K-12.";
RL   J. Bacteriol. 192:4582-4591(2010).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=K12 / BW25113;
RX   PubMed=30498244; DOI=10.1038/s41467-018-07563-6;
RA   Knorr S., Sinn M., Galetskiy D., Williams R.M., Wang C., Mueller N.,
RA   Mayans O., Schleheck D., Hartig J.S.;
RT   "Widespread bacterial lysine degradation proceeding via glutarate and
RT   L-2-hydroxyglutarate.";
RL   Nat. Commun. 9:5071-5071(2018).
RN   [10] {ECO:0000244|PDB:1SF2, ECO:0000244|PDB:1SFF}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
RP   5'-PHOSPHATE OR THE AMINOOXYACETATE INHIBITOR, COFACTOR, AND SUBUNIT.
RC   STRAIN=K12;
RX   PubMed=15323550; DOI=10.1021/bi049218e;
RA   Liu W., Peterson P.E., Carter R.J., Zhou X., Langston J.A.,
RA   Fisher A.J., Toney M.D.;
RT   "Crystal structures of unbound and aminooxyacetate-bound Escherichia
RT   coli gamma-aminobutyrate aminotransferase.";
RL   Biochemistry 43:10896-10905(2004).
RN   [11] {ECO:0000244|PDB:1SZK, ECO:0000244|PDB:1SZS, ECO:0000244|PDB:1SZU}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANTS GLN-50; SER-211 AND
RP   ALA-241 IN COMPLEX WITH PYRIDOXAL 5'-PHOSPHATE, FUNCTION, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT,
RP   MUTAGENESIS OF ILE-50; GLU-211 AND VAL-241, AND REACTION MECHANISM.
RC   STRAIN=K12;
RX   PubMed=15723541; DOI=10.1021/bi048657a;
RA   Liu W., Peterson P.E., Langston J.A., Jin X., Zhou X., Fisher A.J.,
RA   Toney M.D.;
RT   "Kinetic and crystallographic analysis of active site mutants of
RT   Escherichia coli gamma-aminobutyrate aminotransferase.";
RL   Biochemistry 44:2982-2992(2005).
CC   -!- FUNCTION: Pyridoxal phosphate-dependent enzyme that catalyzes
CC       transamination between primary amines and alpha-keto acids.
CC       Catalyzes the transfer of the amino group from gamma-aminobutyrate
CC       (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde
CC       (SSA) and glutamate (PubMed:15723541, PubMed:30498244). Thereby
CC       functions in a GABA degradation pathway that allows some E.coli
CC       strains to utilize GABA as a nitrogen source for growth
CC       (PubMed:12446648). Also catalyzes the conversion of 5-
CC       aminovalerate to glutarate semialdehyde, as part of a L-lysine
CC       degradation pathway that proceeds via cadaverine, glutarate and L-
CC       2-hydroxyglutarate (PubMed:30498244).
CC       {ECO:0000269|PubMed:12446648, ECO:0000269|PubMed:15723541,
CC       ECO:0000269|PubMed:30498244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate +
CC         succinate semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888;
CC         EC=2.6.1.19; Evidence={ECO:0000269|PubMed:15723541,
CC         ECO:0000269|PubMed:30498244};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23353;
CC         Evidence={ECO:0000269|PubMed:12446648};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 5-aminopentanoate = 5-oxopentanoate + L-
CC         glutamate; Xref=Rhea:RHEA:10212, ChEBI:CHEBI:16120,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:356010;
CC         EC=2.6.1.48; Evidence={ECO:0000269|PubMed:30498244};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10213;
CC         Evidence={ECO:0000305|PubMed:30498244};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:15323550,
CC         ECO:0000269|PubMed:15723541};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=197 uM for 4-aminobutanoate (measured for a coupled GabT/GabD
CC         reaction) {ECO:0000269|PubMed:30498244};
CC         KM=439 uM for 5-aminopentanoate (measured for a coupled
CC         GabT/GabD reaction) {ECO:0000269|PubMed:30498244};
CC         KM=5.8 mM for 4-aminobutanoate (at 25 degrees Celsius and pH
CC         7.8) {ECO:0000269|PubMed:15723541};
CC         KM=1.07 mM for 2-oxoglutarate (at 25 degrees Celsius and pH 7.8)
CC         {ECO:0000269|PubMed:15723541};
CC         Note=kcat is 47.4 sec(-1) with 4-aminobutanoate as substrate (at
CC         25 degrees Celsius and pH 7.8). {ECO:0000269|PubMed:15723541};
CC   -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC       {ECO:0000269|PubMed:12446648}.
CC   -!- PATHWAY: Amino-acid degradation. {ECO:0000305|PubMed:30498244}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15323550,
CC       ECO:0000269|PubMed:15723541}.
CC   -!- INDUCTION: Induced by RpoS in response to multiple stress
CC       conditions, including shifts to acidic pH or high osmolarity as
CC       well as starvation or stationary phase. Catabolite repression by
CC       glucose (repression relieved by GABA) (PubMed:14731280). Makes
CC       part of the gabDTPC operon, which is up-regulated by nitrogen
CC       limitation (PubMed:12446648). {ECO:0000269|PubMed:12446648,
CC       ECO:0000269|PubMed:14731280}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not able to
CC       utilize GABA as a nitrogen source, in contrast to wild-type, but
CC       grow normally with arginine, ornithine, putrescine and agmatine
CC       (PubMed:12446648). Cells show only 68% of the wild-type GABA
CC       aminotransferase activity (PubMed:20639325).
CC       {ECO:0000269|PubMed:12446648, ECO:0000269|PubMed:20639325}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
DR   EMBL; M88334; AAC36832.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75709.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16525.1; -; Genomic_DNA.
DR   PIR; A37846; A37846.
DR   RefSeq; NP_417148.1; NC_000913.3.
DR   RefSeq; WP_001087611.1; NZ_LN832404.1.
DR   PDB; 1SF2; X-ray; 2.40 A; A/B/C/D=1-426.
DR   PDB; 1SFF; X-ray; 1.90 A; A/B/C/D=1-426.
DR   PDB; 1SZK; X-ray; 2.52 A; A/B/C/D=1-426.
DR   PDB; 1SZS; X-ray; 2.10 A; A/B/C/D=1-426.
DR   PDB; 1SZU; X-ray; 2.52 A; A/B/C/D=1-426.
DR   PDBsum; 1SF2; -.
DR   PDBsum; 1SFF; -.
DR   PDBsum; 1SZK; -.
DR   PDBsum; 1SZS; -.
DR   PDBsum; 1SZU; -.
DR   ProteinModelPortal; P22256; -.
DR   SMR; P22256; -.
DR   BioGrid; 4259210; 22.
DR   DIP; DIP-9725N; -.
DR   IntAct; P22256; 12.
DR   STRING; 316385.ECDH10B_2829; -.
DR   DrugBank; DB02783; 4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate.
DR   DrugBank; DB02142; Pyridoxamine-5'-Phosphate.
DR   EPD; P22256; -.
DR   jPOST; P22256; -.
DR   PaxDb; P22256; -.
DR   PRIDE; P22256; -.
DR   EnsemblBacteria; AAC75709; AAC75709; b2662.
DR   EnsemblBacteria; BAA16525; BAA16525; BAA16525.
DR   GeneID; 948067; -.
DR   KEGG; ecj:JW2637; -.
DR   KEGG; eco:b2662; -.
DR   PATRIC; fig|1411691.4.peg.4079; -.
DR   EchoBASE; EB0356; -.
DR   EcoGene; EG10361; gabT.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   InParanoid; P22256; -.
DR   KO; K07250; -.
DR   PhylomeDB; P22256; -.
DR   BioCyc; EcoCyc:GABATRANSAM-MONOMER; -.
DR   BioCyc; ECOL316407:JW2637-MONOMER; -.
DR   BioCyc; MetaCyc:GABATRANSAM-MONOMER; -.
DR   BRENDA; 2.6.1.19; 2026.
DR   SABIO-RK; P22256; -.
DR   UniPathway; UPA00733; -.
DR   EvolutionaryTrace; P22256; -.
DR   PRO; PR:P22256; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IDA:EcoCyc.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IDA:EcoCyc.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IGI:EcoCyc.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IMP:EcoCyc.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminotransferase; Complete proteome;
KW   Direct protein sequencing; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN         1    426       4-aminobutyrate aminotransferase GabT.
FT                                /FTId=PRO_0000120384.
FT   REGION      111    112       Pyridoxal phosphate binding.
FT                                {ECO:0000269|PubMed:15323550,
FT                                ECO:0000269|PubMed:15723541}.
FT   BINDING     242    242       Pyridoxal phosphate.
FT                                {ECO:0000269|PubMed:15323550,
FT                                ECO:0000269|PubMed:15723541}.
FT   BINDING     297    297       Pyridoxal phosphate.
FT                                {ECO:0000269|PubMed:15323550,
FT                                ECO:0000269|PubMed:15723541}.
FT   MOD_RES     268    268       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000244|PDB:1SF2,
FT                                ECO:0000244|PDB:1SZS,
FT                                ECO:0000244|PDB:1SZU,
FT                                ECO:0000269|PubMed:15323550,
FT                                ECO:0000269|PubMed:15723541}.
FT   MUTAGEN      50     50       I->Q: 3-fold decrease in catalytic
FT                                activity and 12-fold decrease in affinity
FT                                for GABA. {ECO:0000269|PubMed:15723541}.
FT   MUTAGEN     211    211       E->S: 100-fold decrease in catalytic
FT                                activity and 15-fold decrease in affinity
FT                                for GABA. {ECO:0000269|PubMed:15723541}.
FT   MUTAGEN     241    241       V->A: 25-fold decrease in catalytic
FT                                activity and 5-fold decrease in affinity
FT                                for GABA. {ECO:0000269|PubMed:15723541}.
FT   HELIX         4     14       {ECO:0000244|PDB:1SFF}.
FT   STRAND       22     32       {ECO:0000244|PDB:1SFF}.
FT   STRAND       34     37       {ECO:0000244|PDB:1SFF}.
FT   STRAND       42     47       {ECO:0000244|PDB:1SFF}.
FT   HELIX        48     51       {ECO:0000244|PDB:1SFF}.
FT   HELIX        60     69       {ECO:0000244|PDB:1SFF}.
FT   TURN         70     72       {ECO:0000244|PDB:1SFF}.
FT   TURN         78     80       {ECO:0000244|PDB:1SFF}.
FT   HELIX        84     96       {ECO:0000244|PDB:1SFF}.
FT   STRAND      103    110       {ECO:0000244|PDB:1SFF}.
FT   HELIX       111    126       {ECO:0000244|PDB:1SFF}.
FT   STRAND      130    134       {ECO:0000244|PDB:1SFF}.
FT   HELIX       143    148       {ECO:0000244|PDB:1SFF}.
FT   TURN        153    158       {ECO:0000244|PDB:1SFF}.
FT   STRAND      164    169       {ECO:0000244|PDB:1SFF}.
FT   HELIX       174    176       {ECO:0000244|PDB:1SFF}.
FT   HELIX       180    193       {ECO:0000244|PDB:1SFF}.
FT   HELIX       197    199       {ECO:0000244|PDB:1SFF}.
FT   STRAND      200    205       {ECO:0000244|PDB:1SFF}.
FT   TURN        210    213       {ECO:0000244|PDB:1SFF}.
FT   HELIX       219    232       {ECO:0000244|PDB:1SFF}.
FT   STRAND      235    239       {ECO:0000244|PDB:1SFF}.
FT   TURN        241    248       {ECO:0000244|PDB:1SFF}.
FT   STRAND      249    252       {ECO:0000244|PDB:1SFF}.
FT   HELIX       253    256       {ECO:0000244|PDB:1SFF}.
FT   STRAND      262    266       {ECO:0000244|PDB:1SFF}.
FT   HELIX       268    271       {ECO:0000244|PDB:1SFF}.
FT   STRAND      273    275       {ECO:0000244|PDB:1SZK}.
FT   STRAND      277    282       {ECO:0000244|PDB:1SFF}.
FT   HELIX       283    286       {ECO:0000244|PDB:1SFF}.
FT   STRAND      297    300       {ECO:0000244|PDB:1SFF}.
FT   HELIX       302    317       {ECO:0000244|PDB:1SFF}.
FT   HELIX       320    340       {ECO:0000244|PDB:1SFF}.
FT   STRAND      345    351       {ECO:0000244|PDB:1SFF}.
FT   STRAND      354    360       {ECO:0000244|PDB:1SFF}.
FT   HELIX       361    363       {ECO:0000244|PDB:1SFF}.
FT   HELIX       370    382       {ECO:0000244|PDB:1SFF}.
FT   STRAND      388    391       {ECO:0000244|PDB:1SFF}.
FT   STRAND      396    399       {ECO:0000244|PDB:1SFF}.
FT   HELIX       407    424       {ECO:0000244|PDB:1SFF}.
SQ   SEQUENCE   426 AA;  45775 MW;  02FC80FF0EAA1361 CRC64;
     MNSNKELMQR RSQAIPRGVG QIHPIFADRA ENCRVWDVEG REYLDFAGGI AVLNTGHLHP
     KVVAAVEAQL KKLSHTCFQV LAYEPYLELC EIMNQKVPGD FAKKTLLVTT GSEAVENAVK
     IARAATKRSG TIAFSGAYHG RTHYTLALTG KVNPYSAGMG LMPGHVYRAL YPCPLHGISE
     DDAIASIHRI FKNDAAPEDI AAIVIEPVQG EGGFYASSPA FMQRLRALCD EHGIMLIADE
     VQSGAGRTGT LFAMEQMGVA PDLTTFAKSI AGGFPLAGVT GRAEVMDAVA PGGLGGTYAG
     NPIACVAALE VLKVFEQENL LQKANDLGQK LKDGLLAIAE KHPEIGDVRG LGAMIAIELF
     EDGDHNKPDA KLTAEIVARA RDKGLILLSC GPYYNVLRIL VPLTIEDAQI RQGLEIISQC
     FDEAKQ
//
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