ID A0A1D7MU54_BIFLN Unreviewed; 917 AA. AC A0A1D7MU54; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 08-NOV-2023, entry version 52. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00089, ECO:0000256|HAMAP-Rule:MF_00097}; DE Includes: DE RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE EC=4.1.99.17 {ECO:0000256|HAMAP-Rule:MF_00089}; DE AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000256|HAMAP-Rule:MF_00089}; DE Short=HMP-P synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE Short=HMP-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE Short=HMPP synthase {ECO:0000256|HAMAP-Rule:MF_00089}; DE Includes: DE RecName: Full=Thiamine-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00097}; DE Short=TP synthase {ECO:0000256|HAMAP-Rule:MF_00097}; DE Short=TPS {ECO:0000256|HAMAP-Rule:MF_00097}; DE EC=2.5.1.3 {ECO:0000256|HAMAP-Rule:MF_00097}; DE AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097}; DE Short=TMP pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097}; DE Short=TMP-PPase {ECO:0000256|HAMAP-Rule:MF_00097}; GN Name=thiC {ECO:0000256|HAMAP-Rule:MF_00089, GN ECO:0000313|EMBL:KAB6882449.1}; GN Synonyms=thiE {ECO:0000256|HAMAP-Rule:MF_00097}; GN ORFNames=APC1503_1426 {ECO:0000313|EMBL:PKC88078.1}, CYJ39_05960 GN {ECO:0000313|EMBL:PKY76853.1}, DWV47_07795 GN {ECO:0000313|EMBL:RGW82508.1}, DWV93_02495 GN {ECO:0000313|EMBL:RGW07996.1}, GBB65_01555 GN {ECO:0000313|EMBL:KAB7324170.1}, GBC10_01555 GN {ECO:0000313|EMBL:KAB7284927.1}, GBC26_02320 GN {ECO:0000313|EMBL:KAB7219920.1}, GBC45_02680 GN {ECO:0000313|EMBL:KAB7204130.1}, GBJ95_08160 GN {ECO:0000313|EMBL:KAB6914910.1}, GBJ99_08370 GN {ECO:0000313|EMBL:KAB6908775.1}, GBK03_08495 GN {ECO:0000313|EMBL:KAB6895787.1}, GBK06_08105 GN {ECO:0000313|EMBL:KAB6917606.1}, GBK07_08665 GN {ECO:0000313|EMBL:KAB6882449.1}, GT999_02000 GN {ECO:0000313|EMBL:MZR88099.1}, GUA24_02000 GN {ECO:0000313|EMBL:MZU07821.1}; OS Bifidobacterium longum. OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=216816 {ECO:0000313|EMBL:PKY76853.1, ECO:0000313|Proteomes:UP000234964}; RN [1] {ECO:0000313|EMBL:PKC88078.1, ECO:0000313|Proteomes:UP000232654} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APC1503 {ECO:0000313|EMBL:PKC88078.1, RC ECO:0000313|Proteomes:UP000232654}; RA Arboleya S.; RT "Bifidobacterium longum APC/DPC strains."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:PKY76853.1, ECO:0000313|Proteomes:UP000234964} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMB0788 {ECO:0000313|EMBL:PKY76853.1, RC ECO:0000313|Proteomes:UP000234964}; RA Thomas-White K., Wolfe A.J.; RT "Phylogenetic diversity of female urinary microbiome."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000284732, ECO:0000313|Proteomes:UP000286333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF08-2 {ECO:0000313|EMBL:RGW82508.1, RC ECO:0000313|Proteomes:UP000284732}, and AF13-41 RC {ECO:0000313|EMBL:RGW07996.1, ECO:0000313|Proteomes:UP000286333}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Proteomes:UP000429224, ECO:0000313|Proteomes:UP000429461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIOML-A128 {ECO:0000313|EMBL:KAB7219920.1, RC ECO:0000313|Proteomes:UP000429461}, BIOML-A136 RC {ECO:0000313|EMBL:KAB7204130.1, ECO:0000313|Proteomes:UP000476628}, RC BIOML-A280 {ECO:0000313|EMBL:KAB6914910.1, RC ECO:0000313|Proteomes:UP000474006}, BIOML-A284 RC {ECO:0000313|EMBL:KAB6917606.1, ECO:0000313|Proteomes:UP000491334}, RC BIOML-A286 {ECO:0000313|EMBL:KAB6908775.1, RC ECO:0000313|Proteomes:UP000429224}, BIOML-A290 RC {ECO:0000313|EMBL:KAB6895787.1, ECO:0000313|Proteomes:UP000473438}, RC BIOML-A294 {ECO:0000313|EMBL:KAB6882449.1, RC ECO:0000313|Proteomes:UP000479642}, BIOML-A395 RC {ECO:0000313|EMBL:MZR88099.1, ECO:0000313|Proteomes:UP000466472}, RC BIOML-A409 {ECO:0000313|EMBL:MZU07821.1}, BIOML-A75 RC {ECO:0000313|EMBL:KAB7324170.1, ECO:0000313|Proteomes:UP000451234}, RC and BIOML-A93 {ECO:0000313|EMBL:KAB7284927.1, RC ECO:0000313|Proteomes:UP000476091}; RX PubMed=31477907; DOI=.1038/s41591-019-0559-3; RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X., RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D., RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J., RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A., RA Xavier R.J., Alm E.J.; RT "A library of human gut bacterial isolates paired with longitudinal RT multiomics data enables mechanistic microbiome research."; RL Nat. Med. 25:1442-1452(2019). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) CC in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. CC {ECO:0000256|ARBA:ARBA00003175, ECO:0000256|HAMAP-Rule:MF_00089}. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). CC {ECO:0000256|ARBA:ARBA00003814, ECO:0000256|HAMAP-Rule:MF_00097}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2- CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate CC + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, CC ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3; CC Evidence={ECO:0000256|ARBA:ARBA00000876, ECO:0000256|HAMAP- CC Rule:MF_00097}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl CC phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 CC H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3; CC Evidence={ECO:0000256|ARBA:ARBA00001829, ECO:0000256|HAMAP- CC Rule:MF_00097}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl- CC 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine CC phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, CC ChEBI:CHEBI:58296; EC=2.5.1.3; CC Evidence={ECO:0000256|ARBA:ARBA00001159, ECO:0000256|HAMAP- CC Rule:MF_00097}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L- CC methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'- CC deoxyadenosine + CO + formate + 3 H(+) + L-methionine; CC Xref=Rhea:RHEA:24840, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, CC ChEBI:CHEBI:17245, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844, CC ChEBI:CHEBI:58354, ChEBI:CHEBI:59789, ChEBI:CHEBI:137981; CC EC=4.1.99.17; Evidence={ECO:0000256|HAMAP-Rule:MF_00089}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00097}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00097}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00089}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|HAMAP-Rule:MF_00089}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine CC and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1. CC {ECO:0000256|ARBA:ARBA00005165, ECO:0000256|HAMAP-Rule:MF_00097}. CC -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000256|HAMAP- CC Rule:MF_00089}. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC {ECO:0000256|HAMAP-Rule:MF_00097}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PKY76853.1}. 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; WDZZ01000015; KAB6882449.1; -; Genomic_DNA. DR EMBL; WDZV01000017; KAB6895787.1; -; Genomic_DNA. DR EMBL; WDZR01000018; KAB6908775.1; -; Genomic_DNA. DR EMBL; WDZL01000017; KAB6914910.1; -; Genomic_DNA. DR EMBL; WDZP01000017; KAB6917606.1; -; Genomic_DNA. DR EMBL; WDUB01000002; KAB7204130.1; -; Genomic_DNA. DR EMBL; WDTT01000003; KAB7219920.1; -; Genomic_DNA. DR EMBL; WDSM01000001; KAB7284927.1; -; Genomic_DNA. DR EMBL; WDRV01000001; KAB7324170.1; -; Genomic_DNA. DR EMBL; WXEF01000003; MZR88099.1; -; Genomic_DNA. DR EMBL; WXDR01000003; MZU07821.1; -; Genomic_DNA. DR EMBL; PJDT01000021; PKC88078.1; -; Genomic_DNA. DR EMBL; PKGP01000005; PKY76853.1; -; Genomic_DNA. DR EMBL; QRZU01000002; RGW07996.1; -; Genomic_DNA. DR EMBL; QSAY01000005; RGW82508.1; -; Genomic_DNA. DR RefSeq; WP_011067965.1; NZ_WQQF01000006.1. DR SMR; A0A1D7MU54; -. DR EnsemblBacteria; PKC88078; PKC88078; APC1503_1426. DR EnsemblBacteria; PKD11236; PKD11236; APC1462_1376. DR EnsemblBacteria; PKY76853; PKY76853; CYJ39_05960. DR GeneID; 69578552; -. DR OMA; KASKEWR; -. DR UniPathway; UPA00060; UER00141. DR Proteomes; UP000232654; Unassembled WGS sequence. DR Proteomes; UP000234964; Unassembled WGS sequence. DR Proteomes; UP000284732; Unassembled WGS sequence. DR Proteomes; UP000286333; Unassembled WGS sequence. DR Proteomes; UP000429224; Unassembled WGS sequence. DR Proteomes; UP000429461; Unassembled WGS sequence. DR Proteomes; UP000451234; Unassembled WGS sequence. DR Proteomes; UP000466472; Unassembled WGS sequence. DR Proteomes; UP000473438; Unassembled WGS sequence. DR Proteomes; UP000474006; Unassembled WGS sequence. DR Proteomes; UP000476091; Unassembled WGS sequence. DR Proteomes; UP000476628; Unassembled WGS sequence. DR Proteomes; UP000479642; Unassembled WGS sequence. DR Proteomes; UP000491334; Unassembled WGS sequence. DR Proteomes; UP000638311; Unassembled WGS sequence. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00564; TMP_TenI; 1. DR Gene3D; 6.10.250.620; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 3.20.20.540; Radical SAM ThiC family, central domain; 1. DR HAMAP; MF_00089; ThiC; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR036206; ThiamineP_synth_sf. DR InterPro; IPR022998; ThiamineP_synth_TenI. DR InterPro; IPR037509; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR InterPro; IPR038521; ThiC/Bza_core_dom. DR InterPro; IPR002817; ThiC/BzaA/B. DR InterPro; IPR034291; TMP_synthase. DR NCBIfam; TIGR00190; thiC; 1. DR PANTHER; PTHR30557:SF1; PHOSPHOMETHYLPYRIMIDINE SYNTHASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR30557; THIAMINE BIOSYNTHESIS PROTEIN THIC; 1. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF01964; ThiC_Rad_SAM; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1. DR SFLD; SFLDG01114; phosphomethylpyrimidine_syntha; 1. DR SFLD; SFLDS00113; Radical_SAM_Phosphomethylpyrim; 1. DR SUPFAM; SSF51391; Thiamin phosphate synthase; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00089}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00089}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00089}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00089}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00097}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00097}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_00089}; KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP- KW Rule:MF_00097}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00097}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00089}. FT DOMAIN 19..219 FT /note="Thiamine phosphate synthase/TenI" FT /evidence="ECO:0000259|Pfam:PF02581" FT DOMAIN 327..381 FT /note="ThiC-associated" FT /evidence="ECO:0000259|Pfam:PF13667" FT REGION 256..311 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 276..293 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 48..52 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00097" FT BINDING 84 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00097" FT BINDING 85 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00097" FT BINDING 109 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00097" FT BINDING 128 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00097" FT BINDING 157..159 FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- FT ylidene]ethyl phosphate" FT /ligand_id="ChEBI:CHEBI:62899" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00097" FT BINDING 160 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00097" FT BINDING 196 FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- FT ylidene]ethyl phosphate" FT /ligand_id="ChEBI:CHEBI:62899" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00097" FT BINDING 216..217 FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- FT ylidene]ethyl phosphate" FT /ligand_id="ChEBI:CHEBI:62899" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00097" FT BINDING 487 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 516 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 545 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 581 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 601..603 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 642..645 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 681 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 685 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 708 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 749 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 829 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 832 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" FT BINDING 837 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00089" SQ SEQUENCE 917 AA; 100355 MW; 00000DA28A98E1F6 CRC64; MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI NTICVASEFP VVVGGGVTAA DMAMLADTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM SEKYTAQGGK LYSTAQE //