GLMU_HAEIN
ID GLMU_HAEIN Reviewed; 456 AA.
AC P43889;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631};
DE EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631};
DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631};
GN Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631}; OrderedLocusNames=HI_0642;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP FUNCTION, MUTAGENESIS OF LYS-25; GLN-76; TYR-103; ASP-105; VAL-223 AND
RP GLU-224, REACTION MECHANISM, AND SUBUNIT.
RX PubMed=18029420; DOI=10.1110/ps.073135107;
RA Mochalkin I., Lightle S., Zhu Y., Ohren J.F., Spessard C., Chirgadze N.Y.,
RA Banotai C., Melnick M., McDowell L.;
RT "Characterization of substrate binding and catalysis in the potential
RT antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase
RT (GlmU).";
RL Protein Sci. 16:2657-2666(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP AND SUBUNIT.
RX PubMed=18218712; DOI=10.1110/ps.073271408;
RA Mochalkin I., Lightle S., Narasimhan L., Bornemeier D., Melnick M.,
RA Vanderroest S., McDowell L.;
RT "Structure of a small-molecule inhibitor complexed with GlmU from
RT Haemophilus influenzae reveals an allosteric binding site.";
RL Protein Sci. 17:577-582(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.
RA Melnick M., Mochalkin I., Lightle S., Narasimhan L., Mcdowell L.,
RA Sarver R.;
RT "Discovery and initial sar of quinazoline inhibitors of GlmU from
RT Haemophilus influenzae.";
RL Submitted (OCT-2008) to the PDB data bank.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RX PubMed=22721802; DOI=10.1042/bj20120596;
RA Larsen N.A., Nash T.J., Morningstar M., Shapiro A.B., Joubran C.,
RA Blackett C.J., Patten A.D., Boriack-Sjodin P.A., Doig P.;
RT "An aminoquinazoline inhibitor of the essential bacterial cell wall
RT synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode.";
RL Biochem. J. 446:405-413(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.
RX PubMed=25262942; DOI=10.1016/j.bmc.2014.08.017;
RA Doig P., Boriack-Sjodin P.A., Dumas J., Hu J., Itoh K., Johnson K.,
RA Kazmirski S., Kinoshita T., Kuroda S., Sato T.O., Sugimoto K., Tohyama K.,
RA Aoi H., Wakamatsu K., Wang H.;
RT "Rational design of inhibitors of the bacterial cell wall synthetic enzyme
RT GlmU using virtual screening and lead-hopping.";
RL Bioorg. Med. Chem. 22:6256-6269(2014).
CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de novo
CC biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-
CC terminal domain catalyzes the transfer of acetyl group from acetyl
CC coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-
CC acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into
CC UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-
CC triphosphate), a reaction catalyzed by the N-terminal domain.
CC {ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:18029420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-
CC acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01631};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC alpha-D-glucosamine 6-phosphate (route II): step 2/2.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01631}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631,
CC ECO:0000269|PubMed:18029420, ECO:0000269|PubMed:18218712,
CC ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631,
CC ECO:0000305}.
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DR EMBL; L42023; AAC22302.1; -; Genomic_DNA.
DR PIR; G64083; G64083.
DR RefSeq; NP_438802.1; NC_000907.1.
DR RefSeq; WP_005694502.1; NC_000907.1.
DR PDB; 2V0H; X-ray; 1.79 A; A=1-456.
DR PDB; 2V0I; X-ray; 1.89 A; A=1-456.
DR PDB; 2V0J; X-ray; 2.00 A; A=1-456.
DR PDB; 2V0K; X-ray; 2.30 A; A=1-456.
DR PDB; 2V0L; X-ray; 2.20 A; A=1-456.
DR PDB; 2VD4; X-ray; 1.90 A; A=1-456.
DR PDB; 2W0V; X-ray; 1.99 A; A=1-456.
DR PDB; 2W0W; X-ray; 2.59 A; A=1-456.
DR PDB; 4E1K; X-ray; 2.00 A; A=1-456.
DR PDB; 4KNR; X-ray; 2.10 A; A=1-456.
DR PDB; 4KNX; X-ray; 1.90 A; A=1-456.
DR PDB; 4KPX; X-ray; 2.21 A; A=1-456.
DR PDB; 4KPZ; X-ray; 2.09 A; A=1-456.
DR PDB; 4KQL; X-ray; 2.31 A; A=1-456.
DR PDBsum; 2V0H; -.
DR PDBsum; 2V0I; -.
DR PDBsum; 2V0J; -.
DR PDBsum; 2V0K; -.
DR PDBsum; 2V0L; -.
DR PDBsum; 2VD4; -.
DR PDBsum; 2W0V; -.
DR PDBsum; 2W0W; -.
DR PDBsum; 4E1K; -.
DR PDBsum; 4KNR; -.
DR PDBsum; 4KNX; -.
DR PDBsum; 4KPX; -.
DR PDBsum; 4KPZ; -.
DR PDBsum; 4KQL; -.
DR AlphaFoldDB; P43889; -.
DR SMR; P43889; -.
DR STRING; 71421.HI_0642; -.
DR BindingDB; P43889; -.
DR DrugBank; DB08344; 4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide.
DR EnsemblBacteria; AAC22302; AAC22302; HI_0642.
DR KEGG; hin:HI_0642; -.
DR PATRIC; fig|71421.8.peg.670; -.
DR eggNOG; COG1207; Bacteria.
DR HOGENOM; CLU_029499_15_2_6; -.
DR OMA; TAIVEHK; -.
DR PhylomeDB; P43889; -.
DR BioCyc; HINF71421:G1GJ1-673-MON; -.
DR BRENDA; 2.3.1.157; 2529.
DR BRENDA; 2.7.7.23; 2529.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR EvolutionaryTrace; P43889; -.
DR PRO; PR:P43889; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03353; LbH_GlmU_C; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_01631; GlmU; 1.
DR InterPro; IPR005882; Bifunctional_GlmU.
DR InterPro; IPR038009; GlmU_C_LbH.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 3.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01173; glmU; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nucleotidyltransferase; Peptidoglycan synthesis;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..456
FT /note="Bifunctional protein GlmU"
FT /id="PRO_0000068703"
FT REGION 1..229
FT /note="Pyrophosphorylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 230..250
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 251..456
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 11..14
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:18029420, ECO:0000269|PubMed:22721802,
FT ECO:0000269|PubMed:25262942"
FT BINDING 25
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 76
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:25262942"
FT BINDING 81..82
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:18029420, ECO:0000269|PubMed:25262942"
FT BINDING 103..105
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:18029420, ECO:0000269|PubMed:22721802,
FT ECO:0000269|PubMed:25262942"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 140
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:18029420"
FT BINDING 154
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:18029420"
FT BINDING 169
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:18029420"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 227
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 333
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 351
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 366
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 377
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 380
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P0ACC7, ECO:0000255|HAMAP-
FT Rule:MF_01631"
FT BINDING 386..387
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 405
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 423
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 440
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT MUTAGEN 25
FT /note="K->A: No pyrophosphorylase activity."
FT /evidence="ECO:0000269|PubMed:18029420"
FT MUTAGEN 76
FT /note="Q->A: No pyrophosphorylase activity."
FT /evidence="ECO:0000269|PubMed:18029420"
FT MUTAGEN 103
FT /note="Y->A: Reduces the pyrophosphorylase activity."
FT /evidence="ECO:0000269|PubMed:18029420"
FT MUTAGEN 105
FT /note="D->A: No pyrophosphorylase activity."
FT /evidence="ECO:0000269|PubMed:18029420"
FT MUTAGEN 223
FT /note="V->A: Reduces slightly the pyrophosphorylase
FT activity."
FT /evidence="ECO:0000269|PubMed:18029420"
FT MUTAGEN 224
FT /note="E->A: Reduces the pyrophosphorylase activity."
FT /evidence="ECO:0000269|PubMed:18029420"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:2V0H"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:2V0H"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 229..249
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2V0H"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 276..286
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:2W0W"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 360..372
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:2V0H"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:2V0H"
SQ SEQUENCE 456 AA; 49287 MW; 93B76552A8F9BD36 CRC64;
MTKKALSAVI LAAGKGTRMY SDLPKVLHTI AGKPMVKHVI DTAHQLGSEN IHLIYGHGGD
LMRTHLANEQ VNWVLQTEQL GTAHAVQQAA PFFKDNENIV VLYGDAPLIT KETLEKLIEA
KPENGIALLT VNLDNPTGYG RIIRENGNVV AIVEQKDANA EQLNIKEVNT GVMVSDGASF
KKWLARVGNN NAQGEYYLTD LIALANQDNC QVVAVQATDV MEVEGANNRL QLAALERYFQ
NKQASKLLLE GVMIYDPARF DLRGTLEHGK DVEIDVNVII EGNVKLGDRV KIGTGCVLKN
VVIGNDVEIK PYSVLEDSIV GEKAAIGPFS RLRPGAELAA ETHVGNFVEI KKSTVGKGSK
VNHLTYVGDS EIGSNCNIGA GVITCNYDGA NKFKTIIGDD VFVGSDTQLV APVKVANGAT
IGAGTTITRD VGENELVITR VAQRHIQGWQ RPIKKK
