ID   PUR1_BACSU              Reviewed;         476 AA.
AC   P00497;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE            Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE            EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:6794613};
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE            Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE   Flags: Precursor;
GN   Name=purF {ECO:0000255|HAMAP-Rule:MF_01931,
GN   ECO:0000303|PubMed:6411717}; OrderedLocusNames=BSU06490;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6411717; DOI=10.1016/s0021-9258(17)44497-8;
RA   Makaroff C.A., Zalkin H., Switzer R.L., Vollmer S.J.;
RT   "Cloning of the Bacillus subtilis glutamine phosphoribosylpyrophosphate
RT   amidotransferase gene in Escherichia coli. Nucleotide sequence
RT   determination and properties of the plasmid-encoded enzyme.";
RL   J. Biol. Chem. 258:10586-10593(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3036807; DOI=10.1016/s0021-9258(18)47560-6;
RA   Ebbole D.J., Zalkin H.;
RT   "Cloning and characterization of a 12-gene cluster from Bacillus subtilis
RT   encoding nine enzymes for de novo purine nucleotide synthesis.";
RL   J. Biol. Chem. 262:8274-8287(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 413.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=6794613; DOI=10.1021/bi00523a005;
RA   Wong J.Y., Bernlohr D.A., Turnbough C.L., Switzer R.L.;
RT   "Purification and properties of glutamine phosphoribosylpyrophosphate
RT   amidotransferase from Bacillus subtilis.";
RL   Biochemistry 20:5669-5674(1981).
RN   [6]
RP   ACTIVE SITE, AND PROTEIN SEQUENCE OF 12-35.
RX   PubMed=6411716; DOI=10.1016/s0021-9258(17)44496-6;
RA   Vollmer S.J., Switzer R.L., Hermodson M.A., Bower S.G., Zalkin H.;
RT   "The glutamine-utilizing site of Bacillus subtilis glutamine
RT   phosphoribosylpyrophosphate amidotransferase.";
RL   J. Biol. Chem. 258:10582-10585(1983).
RN   [7]
RP   MUTAGENESIS OF CYS-12.
RX   PubMed=6094545; DOI=10.1016/s0021-9258(18)89882-9;
RA   Maentsaelae P., Zalkin H.;
RT   "Glutamine amidotransferase function. Replacement of the active-site
RT   cysteine in glutamine phosphoribosylpyrophosphate amidotransferase by site-
RT   directed mutagenesis.";
RL   J. Biol. Chem. 259:14230-14236(1984).
RN   [8]
RP   MUTAGENESIS.
RX   PubMed=3090047; DOI=10.1016/s0021-9258(18)67401-0;
RA   Makaroff C.A., Paluh J.L., Zalkin H.;
RT   "Mutagenesis of ligands to the [4 Fe-4S] center of Bacillus subtilis
RT   glutamine phosphoribosylpyrophosphate amidotransferase.";
RL   J. Biol. Chem. 261:11416-11423(1986).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S),
RP   ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=8197456; DOI=10.1126/science.8197456;
RA   Smith J.L., Zaluzec E.J., Wery J.-P., Niu L., Switzer R.L., Zalkin H.,
RA   Satow Y.;
RT   "Structure of the allosteric regulatory enzyme of purine biosynthesis.";
RL   Science 264:1427-1433(1994).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S)
RP   AND MAGNESIUM.
RX   PubMed=9271502; DOI=10.1021/bi9711893;
RA   Chen S., Tomchick D.R., Wolle D., Hu P., Smith J.L., Switzer R.L.,
RA   Zalkin H.;
RT   "Mechanism of the synergistic end-product regulation of Bacillus subtilis
RT   glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides.";
RL   Biochemistry 36:10718-10726(1997).
CC   -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC       phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-
CC       Rule:MF_01931, ECO:0000269|PubMed:6794613}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC         Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01931, ECO:0000269|PubMed:6794613};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01931, ECO:0000269|PubMed:9271502};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01931,
CC       ECO:0000269|PubMed:9271502};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:8197456};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The [4Fe-4S] cluster
CC       requires a potential lower than -600 mV for reduction.
CC       {ECO:0000269|PubMed:8197456};
CC   -!- ACTIVITY REGULATION: Allosterically regulated; subject to end product
CC       regulation by purine nucleotides. {ECO:0000269|PubMed:8197456}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC       (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC       diphosphate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01931}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8197456}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01931,
CC       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; J02732; AAA22680.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12469.2; -; Genomic_DNA.
DR   PIR; A00582; XQBS.
DR   RefSeq; NP_388531.2; NC_000964.3.
DR   RefSeq; WP_003233947.1; NZ_JNCM01000032.1.
DR   PDB; 1AO0; X-ray; 2.80 A; A/B/C/D=12-470.
DR   PDB; 1GPH; X-ray; 3.00 A; 1/2/3/4=12-476.
DR   PDBsum; 1AO0; -.
DR   PDBsum; 1GPH; -.
DR   AlphaFoldDB; P00497; -.
DR   SMR; P00497; -.
DR   IntAct; P00497; 1.
DR   MINT; P00497; -.
DR   STRING; 224308.BSU06490; -.
DR   DrugBank; DB01972; Guanosine-5'-Monophosphate.
DR   MEROPS; C44.001; -.
DR   PaxDb; 224308-BSU06490; -.
DR   EnsemblBacteria; CAB12469; CAB12469; BSU_06490.
DR   GeneID; 83883911; -.
DR   GeneID; 936046; -.
DR   KEGG; bsu:BSU06490; -.
DR   PATRIC; fig|224308.179.peg.705; -.
DR   eggNOG; COG0034; Bacteria.
DR   InParanoid; P00497; -.
DR   OrthoDB; 9801213at2; -.
DR   PhylomeDB; P00497; -.
DR   BioCyc; BSUB:BSU06490-MONOMER; -.
DR   BRENDA; 2.4.2.14; 658.
DR   UniPathway; UPA00074; UER00124.
DR   EvolutionaryTrace; P00497; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR   CDD; cd00715; GPATase_N; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   HAMAP; MF_01931; PurF; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005854; PurF.
DR   InterPro; IPR035584; PurF_N.
DR   NCBIfam; TIGR01134; purF; 1.
DR   PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Allosteric enzyme; Direct protein sequencing;
KW   Glutamine amidotransferase; Glycosyltransferase; Iron; Iron-sulfur;
KW   Magnesium; Metal-binding; Purine biosynthesis; Reference proteome;
KW   Transferase.
FT   PROPEP          1..11
FT                   /evidence="ECO:0000269|PubMed:6411716"
FT                   /id="PRO_0000029251"
FT   CHAIN           12..476
FT                   /note="Amidophosphoribosyltransferase"
FT                   /id="PRO_0000029252"
FT   DOMAIN          12..231
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   ACT_SITE        12
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT                   ECO:0000269|PubMed:6411716"
FT   BINDING         247
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT                   ECO:0000269|PubMed:8197456, ECO:0000269|PubMed:9271502"
FT   BINDING         294
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT                   ECO:0000269|PubMed:9271502"
FT   BINDING         356
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT                   ECO:0000269|PubMed:9271502"
FT   BINDING         357
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT                   ECO:0000269|PubMed:9271502"
FT   BINDING         393
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT                   ECO:0000269|PubMed:8197456, ECO:0000269|PubMed:9271502"
FT   BINDING         448
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT                   ECO:0000269|PubMed:8197456, ECO:0000269|PubMed:9271502"
FT   BINDING         451
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT                   ECO:0000269|PubMed:8197456, ECO:0000269|PubMed:9271502"
FT   MUTAGEN         12
FT                   /note="C->F: Loss of enzyme activity and N-terminal
FT                   processing."
FT                   /evidence="ECO:0000269|PubMed:6094545"
FT   MUTAGEN         394
FT                   /note="F->V: Partial loss of activity."
FT                   /evidence="ECO:0000269|PubMed:3090047"
FT   MUTAGEN         442
FT                   /note="D->S: Partial loss of activity."
FT                   /evidence="ECO:0000269|PubMed:3090047"
FT   MUTAGEN         448
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:3090047"
FT   MUTAGEN         451
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:3090047"
FT   MUTAGEN         452
FT                   /note="F->C: Lethal."
FT                   /evidence="ECO:0000269|PubMed:3090047"
FT   CONFLICT        413
FT                   /note="E -> G (in Ref. 1 and 2; AAA22680)"
FT                   /evidence="ECO:0000305"
FT   STRAND          13..19
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           23..33
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           34..37
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          40..47
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          52..59
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           61..64
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:1GPH"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          75..83
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:1GPH"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          108..116
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           119..128
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          133..135
FT                   /evidence="ECO:0007829|PDB:1GPH"
FT   HELIX           138..147
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           154..162
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          167..174
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          176..183
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          192..196
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          199..205
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           207..212
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          215..219
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          224..229
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          232..238
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           248..252
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           266..281
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          286..289
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   TURN            292..295
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           296..306
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          314..316
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           329..334
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          338..342
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           344..347
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          351..357
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          360..362
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           363..374
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          378..386
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   TURN            397..399
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   TURN            407..409
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           412..419
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   STRAND          422..426
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           429..436
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   TURN            443..446
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           450..453
FT                   /evidence="ECO:0007829|PDB:1AO0"
FT   HELIX           467..469
FT                   /evidence="ECO:0007829|PDB:1AO0"
SQ   SEQUENCE   476 AA;  51692 MW;  6BC2FDA3288002F0 CRC64;
     MLAEIKGLNE ECGVFGIWGH EEAPQITYYG LHSLQHRGQE GAGIVATDGE KLTAHKGQGL
     ITEVFQNGEL SKVKGKGAIG HVRYATAGGG GYENVQPLLF RSQNNGSLAL AHNGNLVNAT
     QLKQQLENQG SIFQTSSDTE VLAHLIKRSG HFTLKDQIKN SLSMLKGAYA FLIMTETEMI
     VALDPNGLRP LSIGMMGDAY VVASETCAFD VVGATYLREV EPGEMLIIND EGMKSERFSM
     NINRSICSME YIYFSRPDSN IDGINVHSAR KNLGKMLAQE SAVEADVVTG VPDSSISAAI
     GYAEATGIPY ELGLIKNRYV GRTFIQPSQA LREQGVRMKL SAVRGVVEGK RVVMVDDSIV
     RGTTSRRIVT MLREAGATEV HVKISSPPIA HPCFYGIDTS THEELIASSH SVEEIRQEIG
     ADTLSFLSVE GLLKGIGRKY DDSNCGQCLA CFTGKYPTEI YQDTVLPHVK EAVLTK
//