ID   PAT_ECOLI               Reviewed;         459 AA.
AC   P42588; P78108; Q2M9D3; Q46873;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   27-NOV-2024, entry version 170.
DE   RecName: Full=Putrescine aminotransferase {ECO:0000303|PubMed:12617754};
DE            Short=PAT;
DE            Short=PATase {ECO:0000303|PubMed:25423189};
DE            EC=2.6.1.82 {ECO:0000269|PubMed:12617754, ECO:0000269|PubMed:3510672};
DE   AltName: Full=Cadaverine transaminase {ECO:0000305|PubMed:12617754};
DE   AltName: Full=Diamine transaminase;
DE            EC=2.6.1.29 {ECO:0000269|PubMed:12617754, ECO:0000269|PubMed:30498244, ECO:0000269|PubMed:3510672, ECO:0000305|PubMed:28522202};
DE   AltName: Full=Putrescine transaminase {ECO:0000305|PubMed:12617754};
DE   AltName: Full=Putrescine--2-oxoglutaric acid transaminase;
DE   AltName: Full=Putrescine:2-OG aminotransferase {ECO:0000303|PubMed:12617754};
GN   Name=patA {ECO:0000303|PubMed:22636776}; Synonyms=ygjG;
GN   OrderedLocusNames=b3073, JW5510;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
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., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
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 MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX   PubMed=3510672; DOI=10.1016/0304-4165(86)90085-1;
RA   Prieto-Santos M.I., Martin-Checa J., Balana-Fouce R., Garrido-Pertierra A.;
RT   "A pathway for putrescine catabolism in Escherichia coli.";
RL   Biochim. Biophys. Acta 880:242-244(1986).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF START CODON,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND INDUCTION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=12617754; DOI=10.1186/1471-2180-3-2;
RA   Samsonova N.N., Smirnov S.V., Altman I.B., Ptitsyn L.R.;
RT   "Molecular cloning and characterization of Escherichia coli K12 ygjG
RT   gene.";
RL   BMC Microbiol. 3:2-2(2003).
RN   [5]
RP   SUBUNIT.
RC   STRAIN=K12;
RX   PubMed=22949197; DOI=10.1107/s1744309112030886;
RA   Yeo S.J., Jeong J.H., Yu S.N., Kim Y.G.;
RT   "Crystallization and preliminary X-ray crystallographic analysis of YgjG
RT   from Escherichia coli.";
RL   Acta Crystallogr. F 68:1070-1072(2012).
RN   [6]
RP   FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=22636776; DOI=10.1128/jb.05063-11;
RA   Schneider B.L., Reitzer L.;
RT   "Pathway and enzyme redundancy in putrescine catabolism in Escherichia
RT   coli.";
RL   J. Bacteriol. 194:4080-4088(2012).
RN   [7]
RP   INDUCTION.
RX   PubMed=24906570; DOI=10.1007/s00203-014-0991-1;
RA   Kim Y.S., Shin H.C., Lee J.H.;
RT   "Two mechanisms for putrescine-dependent transcriptional expression of the
RT   putrescine aminotransferase gene, ygjG, in Escherichia coli.";
RL   Arch. Microbiol. 196:611-618(2014).
RN   [8]
RP   BIOTECHNOLOGY, AND CATALYTIC ACTIVITY.
RX   PubMed=28522202; DOI=10.1016/j.biortech.2017.04.108;
RA   Jorge J.M.P., Perez-Garcia F., Wendisch V.F.;
RT   "A new metabolic route for the fermentative production of 5-aminovalerate
RT   from glucose and alternative carbon sources.";
RL   Bioresour. Technol. 245:1701-1709(2017).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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 L-2-
RT   hydroxyglutarate.";
RL   Nat. Commun. 9:5071-5071(2018).
RN   [10] {ECO:0007744|PDB:4UOX, ECO:0007744|PDB:4UOY}
RP   X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) IN COMPLEXES WITH PUTRESCINE AND
RP   PLP, COFACTOR, AND PYRIDOXAL-PHOSPHATE AT LYS-300.
RX   PubMed=25423189; DOI=10.1371/journal.pone.0113212;
RA   Cha H.J., Jeong J.H., Rojviriya C., Kim Y.G.;
RT   "Structure of putrescine aminotransferase from Escherichia coli provides
RT   insights into the substrate specificity among class III
RT   aminotransferases.";
RL   PLoS ONE 9:E113212-E113212(2014).
RN   [11] {ECO:0007744|PDB:5H7D, ECO:0007744|PDB:5X3F}
RP   X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 7-453.
RX   PubMed=28572639; DOI=10.1038/s41598-017-02803-z;
RA   Youn S.J., Kwon N.Y., Lee J.H., Kim J.H., Choi J., Lee H., Lee J.O.;
RT   "Construction of novel repeat proteins with rigid and predictable
RT   structures using a shared helix method.";
RL   Sci. Rep. 7:2595-2595(2017).
CC   -!- FUNCTION: Catalyzes the aminotransferase reaction from putrescine to 2-
CC       oxoglutarate, leading to glutamate and 4-aminobutanal, which
CC       spontaneously cyclizes to form 1-pyrroline (PubMed:12617754,
CC       PubMed:3510672). This is the first step in one of two pathways for
CC       putrescine degradation, where putrescine is converted into 4-
CC       aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal, which
CC       allows E.coli to grow on putrescine as the sole nitrogen source
CC       (PubMed:22636776, PubMed:3510672). Also functions as a cadaverine
CC       transaminase in a a L-lysine degradation pathway to succinate that
CC       proceeds via cadaverine, glutarate and L-2-hydroxyglutarate
CC       (PubMed:12617754, PubMed:30498244). Is also able to transaminate
CC       spermidine, in lower extent, but not ornithine. Alpha-ketobutyrate and
CC       pyruvate can also act as amino acceptors, although much less
CC       efficiently (PubMed:12617754). {ECO:0000269|PubMed:12617754,
CC       ECO:0000269|PubMed:22636776, ECO:0000269|PubMed:30498244,
CC       ECO:0000269|PubMed:3510672}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alkane-alpha,omega-diamine + 2-oxoglutarate = an omega-
CC         aminoaldehyde + L-glutamate; Xref=Rhea:RHEA:18217, Rhea:RHEA-
CC         COMP:9766, Rhea:RHEA-COMP:12750, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:70977, ChEBI:CHEBI:133427;
CC         EC=2.6.1.29; Evidence={ECO:0000269|PubMed:12617754,
CC         ECO:0000269|PubMed:30498244, ECO:0000269|PubMed:3510672,
CC         ECO:0000305|PubMed:28522202};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18218;
CC         Evidence={ECO:0000305|PubMed:12617754, ECO:0000305|PubMed:30498244,
CC         ECO:0000305|PubMed:3510672};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=putrescine + 2-oxoglutarate = 1-pyrroline + L-glutamate + H2O;
CC         Xref=Rhea:RHEA:12268, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:36781, ChEBI:CHEBI:326268;
CC         EC=2.6.1.82; Evidence={ECO:0000269|PubMed:12617754,
CC         ECO:0000269|PubMed:3510672};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12269;
CC         Evidence={ECO:0000305|PubMed:12617754, ECO:0000305|PubMed:3510672};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cadaverine + 2-oxoglutarate = 5-aminopentanal + L-glutamate;
CC         Xref=Rhea:RHEA:61624, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58384, ChEBI:CHEBI:144896;
CC         Evidence={ECO:0000269|PubMed:12617754, ECO:0000269|PubMed:30498244,
CC         ECO:0000305|PubMed:28522202};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61625;
CC         Evidence={ECO:0000305|PubMed:30498244};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:25423189};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=22.5 uM for putrescine {ECO:0000269|PubMed:3510672};
CC       pH dependence:
CC         Optimum pH is 7.2 (PubMed:3510672). Optimum pH is 9.0. Active at
CC         alkaline pH. {ECO:0000269|PubMed:12617754,
CC         ECO:0000269|PubMed:3510672};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. Highly active from 20 to
CC         80 degrees Celsius. {ECO:0000269|PubMed:12617754};
CC   -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC       aminobutanal from putrescine (transaminase route): step 1/1.
CC       {ECO:0000269|PubMed:22636776, ECO:0000269|PubMed:3510672}.
CC   -!- PATHWAY: Amino-acid degradation. {ECO:0000305|PubMed:30498244}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22949197}.
CC   -!- INDUCTION: Up-regulated under nitrogen starvation conditions.
CC       Expression is sigma-54-dependent (PubMed:12617754). Up-regulated by
CC       putrescine; this gene expression regulation is controlled by at least
CC       two sigma factors: rpoS under excess nitrogen conditions and rpoN under
CC       nitrogen-starvation conditions (PubMed:24906570).
CC       {ECO:0000269|PubMed:12617754, ECO:0000269|PubMed:24906570}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a high decrease in
CC       putrescine aminotransferase activity, but are still able to grow with
CC       putrescine as the sole nitrogen source. However, a mutant lacking both
CC       patA and either puuA, puuB or puuC cannot grow with putrescine as the
CC       sole nitrogen source. {ECO:0000269|PubMed:22636776}.
CC   -!- BIOTECHNOLOGY: Can be used in the industrial production of the value-
CC       added compound 5-aminovalerate. {ECO:0000269|PubMed:28522202}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. Putrescine aminotransferase subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA57874.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAA89152.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE77123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U18997; AAA57874.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U28379; AAA89152.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76108.3; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77123.1; ALT_INIT; Genomic_DNA.
DR   PIR; F65095; F65095.
DR   RefSeq; NP_417544.5; NC_000913.3.
DR   RefSeq; WP_001301395.1; NZ_LN832404.1.
DR   PDB; 4UOX; X-ray; 2.08 A; A/B/C/D=1-459.
DR   PDB; 4UOY; X-ray; 2.30 A; A/B/C/D=1-459.
DR   PDB; 5H7D; X-ray; 2.57 A; A/B/C/D/I/J/M/N=7-453.
DR   PDB; 5X3F; X-ray; 3.38 A; A=7-453.
DR   PDB; 8CPL; X-ray; 1.60 A; A/B/C/D=7-457.
DR   PDBsum; 4UOX; -.
DR   PDBsum; 4UOY; -.
DR   PDBsum; 5H7D; -.
DR   PDBsum; 5X3F; -.
DR   PDBsum; 8CPL; -.
DR   AlphaFoldDB; P42588; -.
DR   SMR; P42588; -.
DR   BioGRID; 4262398; 14.
DR   DIP; DIP-12233N; -.
DR   IntAct; P42588; 1.
DR   MINT; P42588; -.
DR   STRING; 511145.b3073; -.
DR   jPOST; P42588; -.
DR   PaxDb; 511145-b3073; -.
DR   EnsemblBacteria; AAC76108; AAC76108; b3073.
DR   GeneID; 947120; -.
DR   KEGG; ecj:JW5510; -.
DR   KEGG; eco:b3073; -.
DR   KEGG; ecoc:C3026_16785; -.
DR   PATRIC; fig|511145.12.peg.3167; -.
DR   EchoBASE; EB2577; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   InParanoid; P42588; -.
DR   OMA; KWFAFQH; -.
DR   PhylomeDB; P42588; -.
DR   BioCyc; EcoCyc:G7596-MONOMER; -.
DR   BioCyc; MetaCyc:G7596-MONOMER; -.
DR   BRENDA; 2.6.1.82; 2026.
DR   SABIO-RK; P42588; -.
DR   UniPathway; UPA00188; UER00290.
DR   EvolutionaryTrace; P42588; -.
DR   PRO; PR:P42588; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0019161; F:diamine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0033094; F:putrescine--2-oxoglutarate transaminase activity; IDA:EcoCyc.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR   GO; GO:0019477; P:L-lysine catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009447; P:putrescine catabolic process; IDA:EcoCyc.
DR   CDD; cd00610; OAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000004; Acetylornithine aminotransferase; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_01276; Putres_aminotrans_3; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR050103; Class-III_PLP-dep_AT.
DR   InterPro; IPR017747; Putrescine_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03372; putres_am_tran; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF112; PUTRESCINE AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminotransferase; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..459
FT                   /note="Putrescine aminotransferase"
FT                   /id="PRO_0000120507"
FT   BINDING         150..151
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:25423189"
FT   BINDING         274
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:25423189"
FT   BINDING         332
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000269|PubMed:25423189"
FT   MOD_RES         300
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:25423189,
FT                   ECO:0007744|PDB:4UOY"
FT   HELIX           10..22
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           28..45
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           48..56
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          83..88
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   TURN            89..93
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           101..113
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          119..122
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           124..136
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          141..149
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           150..165
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   TURN            166..169
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           185..190
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           194..197
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           198..200
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          207..210
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           215..228
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          232..237
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   TURN            242..245
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           253..264
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          267..271
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   TURN            273..280
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          281..284
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           285..287
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   TURN            288..290
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           300..303
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   TURN            304..306
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          310..315
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           316..319
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           320..322
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:4UOY"
FT   HELIX           337..352
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           355..376
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   TURN            378..380
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          381..387
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          390..397
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           398..410
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   STRAND          416..418
FT                   /evidence="ECO:0007829|PDB:4UOY"
FT   STRAND          419..427
FT                   /evidence="ECO:0007829|PDB:4UOX"
FT   HELIX           435..456
FT                   /evidence="ECO:0007829|PDB:4UOX"
SQ   SEQUENCE   459 AA;  49661 MW;  0B4D42A24627335D CRC64;
     MNRLPSSASA LACSAHALNL IEKRTLDHEE MKALNREVIE YFKEHVNPGF LEYRKSVTAG
     GDYGAVEWQA GSLNTLVDTQ GQEFIDCLGG FGIFNVGHRN PVVVSAVQNQ LAKQPLHSQE
     LLDPLRAMLA KTLAALTPGK LKYSFFCNSG TESVEAALKL AKAYQSPRGK FTFIATSGAF
     HGKSLGALSA TAKSTFRKPF MPLLPGFRHV PFGNIEAMRT ALNECKKTGD DVAAVILEPI
     QGEGGVILPP PGYLTAVRKL CDEFGALMIL DEVQTGMGRT GKMFACEHEN VQPDILCLAK
     ALGGGVMPIG ATIATEEVFS VLFDNPFLHT TTFGGNPLAC AAALATINVL LEQNLPAQAE
     QKGDMLLDGF RQLAREYPDL VQEARGKGML MAIEFVDNEI GYNFASEMFR QRVLVAGTLN
     NAKTIRIEPP LTLTIEQCEL VIKAARKALA AMRVSVEEA
//