CGOX_BACSU
ID CGOX_BACSU Reviewed; 470 AA.
AC P32397;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000305};
DE EC=1.3.3.15 {ECO:0000269|PubMed:7928957, ECO:0000269|PubMed:8288631, ECO:0000269|PubMed:9217019, ECO:0000269|PubMed:9784236};
GN Name=cgoX {ECO:0000303|PubMed:28123057};
GN Synonyms=hemG {ECO:0000303|PubMed:8288631},
GN hemY {ECO:0000303|PubMed:1459957}; OrderedLocusNames=BSU10140;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RX PubMed=1459957; DOI=10.1128/jb.174.24.8081-8093.1992;
RA Hansson M., Hederstedt L.;
RT "Cloning and characterization of the Bacillus subtilis hemEHY gene cluster,
RT which encodes protoheme IX biosynthetic enzymes.";
RL J. Bacteriol. 174:8081-8093(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
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 PROTEIN SEQUENCE OF 2-8, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=7928957; DOI=10.1128/jb.176.19.5962-5970.1994;
RA Hansson M., Hederstedt L.;
RT "Bacillus subtilis HemY is a peripheral membrane protein essential for
RT protoheme IX synthesis which can oxidize coproporphyrinogen III and
RT protoporphyrinogen IX.";
RL J. Bacteriol. 176:5962-5970(1994).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBUNIT, SUBCELLULAR LOCATION, AND COFACTOR.
RX PubMed=8288631; DOI=10.1016/s0021-9258(17)42182-x;
RA Dailey T.A., Meissner P., Dailey H.A.;
RT "Expression of a cloned protoporphyrinogen oxidase.";
RL J. Biol. Chem. 269:813-815(1994).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=9217019; DOI=10.1016/s0167-4838(97)00030-7;
RA Hansson M., Gustafsson M.C., Kannangara C.G., Hederstedt L.;
RT "Isolated Bacillus subtilis HemY has coproporphyrinogen III to
RT coproporphyrin III oxidase activity.";
RL Biochim. Biophys. Acta 1340:97-104(1997).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=9784236; DOI=10.1006/abbi.1998.0834;
RA Corrigall A.V., Siziba K.B., Maneli M.H., Shephard E.G., Ziman M.,
RA Dailey T.A., Dailey H.A., Kirsch R.E., Meissner P.N.;
RT "Purification of and kinetic studies on a cloned protoporphyrinogen oxidase
RT from the aerobic bacterium Bacillus subtilis.";
RL Arch. Biochem. Biophys. 358:251-256(1998).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF TYR-366.
RX PubMed=19266155; DOI=10.1007/s00726-009-0256-5;
RA Sun L., Wen X., Tan Y., Li H., Yang X., Zhao Y., Wang B., Cao Q., Niu C.,
RA Xi Z.;
RT "Site-directed mutagenesis and computational study of the Y366 active site
RT in Bacillus subtilis protoporphyrinogen oxidase.";
RL Amino Acids 37:523-530(2009).
RN [9]
RP PATHWAY, AND REVIEW.
RX PubMed=25711532; DOI=10.1016/j.abb.2015.02.017;
RA Dailey H.A., Gerdes S.;
RT "HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme
RT synthesis in Firmicutes and Actinobacteria.";
RL Arch. Biochem. Biophys. 574:27-35(2015).
RN [10]
RP NOMENCLATURE, AND REVIEW.
RX PubMed=28123057; DOI=10.1128/mmbr.00048-16;
RA Dailey H.A., Dailey T.A., Gerdes S., Jahn D., Jahn M., O'Brian M.R.,
RA Warren M.J.;
RT "Prokaryotic heme biosynthesis: multiple pathways to a common essential
RT product.";
RL Microbiol. Mol. Biol. Rev. 81:e00048-e00048(2017).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH FAD AND THE INHIBITOR
RP ACIFLUORFEN, FUNCTION, COFACTOR, ACTIVITY REGULATION, MUTAGENESIS OF
RP PRO-64; LYS-71; ILE-176 AND PHE-227, AND SUBUNIT.
RX PubMed=19944166; DOI=10.1016/j.jsb.2009.11.012;
RA Qin X., Sun L., Wen X., Yang X., Tan Y., Jin H., Cao Q., Zhou W., Xi Z.,
RA Shen Y.;
RT "Structural insight into unique properties of protoporphyrinogen oxidase
RT from Bacillus subtilis.";
RL J. Struct. Biol. 170:76-82(2010).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis
CC (PubMed:7928957, PubMed:9217019). Catalyzes the oxidation of
CC coproporphyrinogen III to coproporphyrin III (PubMed:8288631,
CC PubMed:7928957, PubMed:9217019, PubMed:9784236). Can also oxidize
CC protoporphyrinogen IX to protoporphyrin-IX (PubMed:8288631,
CC PubMed:7928957, PubMed:9217019, PubMed:9784236, PubMed:19944166). The
CC specific activity for the oxidation of coproporphyrinogen III is much
CC higher than that for the oxidation of protoporphyrinogen IX
CC (PubMed:7928957, PubMed:9217019). Can also oxidize mesoporphyrinogen
CC IX, but not uroporphyrinogen III (PubMed:8288631, PubMed:9784236,
CC PubMed:7928957). {ECO:0000269|PubMed:19944166,
CC ECO:0000269|PubMed:7928957, ECO:0000269|PubMed:8288631,
CC ECO:0000269|PubMed:9217019, ECO:0000269|PubMed:9784236}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2;
CC Xref=Rhea:RHEA:43436, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57309, ChEBI:CHEBI:131725; EC=1.3.3.15;
CC Evidence={ECO:0000269|PubMed:7928957, ECO:0000269|PubMed:8288631,
CC ECO:0000269|PubMed:9217019, ECO:0000269|PubMed:9784236};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43437;
CC Evidence={ECO:0000269|PubMed:7928957, ECO:0000269|PubMed:8288631,
CC ECO:0000269|PubMed:9217019, ECO:0000269|PubMed:9784236};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19944166, ECO:0000269|PubMed:8288631,
CC ECO:0000269|PubMed:9217019, ECO:0000269|PubMed:9784236};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:19944166};
CC -!- ACTIVITY REGULATION: Only weakly inhibited by acifluorfen, in contrast
CC to eukaryotic family members (PubMed:8288631, PubMed:9784236,
CC PubMed:19944166). Weakly inhibited by methylacifluorfen
CC (PubMed:9784236). Bilirubin, biliverdin and hemin are all competitive
CC inhibitors (PubMed:9784236). {ECO:0000269|PubMed:19944166,
CC ECO:0000269|PubMed:8288631, ECO:0000269|PubMed:9784236}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.56 uM for coproporphyrinogen III {ECO:0000269|PubMed:7928957};
CC KM=5.29 uM for coproporphyrinogen III {ECO:0000269|PubMed:9784236};
CC KM=0.95 uM for protoporphyrinogen IX {ECO:0000269|PubMed:7928957};
CC KM=10.4 uM for protoporphyrinogen IX {ECO:0000269|PubMed:8288631};
CC KM=1.0 uM for protoporphyrinogen IX {ECO:0000269|PubMed:9784236};
CC KM=21.1 uM for mesoporphyrinogen IX {ECO:0000269|PubMed:8288631};
CC KM=4.92 uM for mesoporphyrinogen IX {ECO:0000269|PubMed:9784236};
CC Vmax=7.0 nmol/min/mg enzyme with coproporphyrinogen III as substrate
CC {ECO:0000269|PubMed:7928957};
CC Vmax=0.98 nmol/min/mg enzyme with coproporphyrinogen III as substrate
CC {ECO:0000269|PubMed:9784236};
CC Vmax=0.85 nmol/min/mg enzyme with protoporphyrinogen IX as substrate
CC {ECO:0000269|PubMed:7928957};
CC Vmax=3.7 nmol/min/mg enzyme with protoporphyrinogen IX as substrate
CC {ECO:0000269|PubMed:9784236};
CC Vmax=45 nmol/min/mg enzyme with mesoporphyrinogen IX as substrate
CC {ECO:0000269|PubMed:9784236};
CC Note=kcat is 0.05 min(-1) with coproporphyrinogen III as substrate
CC (PubMed:9784236). kcat is 0.19 min(-1) with protoporphyrinogen IX as
CC substrate (PubMed:9784236). kcat is 2.69 min(-1) with
CC mesoporphyrinogen IX as substrate (PubMed:9784236).
CC {ECO:0000269|PubMed:9784236};
CC pH dependence:
CC Optimum pH is 8.7 (for protoporphyrinogen oxidation).
CC {ECO:0000269|PubMed:9784236};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000269|PubMed:1459957, ECO:0000269|PubMed:7928957,
CC ECO:0000305|PubMed:25711532}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19944166,
CC ECO:0000269|PubMed:8288631, ECO:0000269|PubMed:9784236}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8288631}. Cell
CC membrane {ECO:0000269|PubMed:7928957}; Peripheral membrane protein
CC {ECO:0000269|PubMed:7928957}.
CC -!- DISRUPTION PHENOTYPE: Mutations cause the accumulation of
CC coproporphyrinogen III or coproporphyrin III in the growth medium and
CC the accumulation of trace amounts of other porphyrinogens or porphyrins
CC intracellularly. {ECO:0000269|PubMed:7928957}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Coproporphyrinogen III oxidase subfamily.
CC {ECO:0000305}.
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DR EMBL; M97208; AAA22519.1; -; Genomic_DNA.
DR EMBL; Y14083; CAA74520.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12854.1; -; Genomic_DNA.
DR PIR; D47045; D47045.
DR RefSeq; NP_388895.1; NC_000964.3.
DR RefSeq; WP_003245394.1; NZ_JNCM01000035.1.
DR PDB; 3I6D; X-ray; 2.90 A; A/B=1-470.
DR PDBsum; 3I6D; -.
DR AlphaFoldDB; P32397; -.
DR SMR; P32397; -.
DR STRING; 224308.BSU10140; -.
DR BindingDB; P32397; -.
DR ChEMBL; CHEMBL1075048; -.
DR DrugBank; DB07338; Acifluorfen.
DR jPOST; P32397; -.
DR PaxDb; P32397; -.
DR PRIDE; P32397; -.
DR DNASU; 936311; -.
DR EnsemblBacteria; CAB12854; CAB12854; BSU_10140.
DR GeneID; 936311; -.
DR KEGG; bsu:BSU10140; -.
DR PATRIC; fig|224308.179.peg.1090; -.
DR eggNOG; COG1232; Bacteria.
DR InParanoid; P32397; -.
DR OMA; WFDQWFG; -.
DR PhylomeDB; P32397; -.
DR BioCyc; BSUB:BSU10140-MON; -.
DR BioCyc; MetaCyc:BSU10140-MON; -.
DR BRENDA; 1.3.3.15; 658.
DR BRENDA; 1.3.3.4; 658.
DR SABIO-RK; P32397; -.
DR UniPathway; UPA00252; -.
DR EvolutionaryTrace; P32397; -.
DR PRO; PR:P32397; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00562; proto_IX_ox; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Direct protein sequencing; FAD;
KW Flavoprotein; Heme biosynthesis; Membrane; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..470
FT /note="Coproporphyrinogen III oxidase"
FT /id="PRO_0000135263"
FT BINDING 12..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19944166"
FT BINDING 41..42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19944166"
FT BINDING 49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19944166"
FT BINDING 63..66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19944166"
FT BINDING 256
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P56601"
FT BINDING 409
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19944166"
FT BINDING 448..450
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19944166"
FT MUTAGEN 64
FT /note="P->A: Decreased affinity for protoporphyrinogen-IX."
FT /evidence="ECO:0000269|PubMed:19944166"
FT MUTAGEN 71
FT /note="K->A: Strongly decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:19944166"
FT MUTAGEN 176
FT /note="I->A: Strongly decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:19944166"
FT MUTAGEN 227
FT /note="F->R: Decreased affinity for protoporphyrinogen-IX."
FT /evidence="ECO:0000269|PubMed:19944166"
FT MUTAGEN 366
FT /note="Y->A,H: Reduces protoporphyrinogen oxidation by
FT 90%."
FT /evidence="ECO:0000269|PubMed:19266155"
FT MUTAGEN 366
FT /note="Y->E: Reduces protoporphyrinogen oxidation by 99%."
FT /evidence="ECO:0000269|PubMed:19266155"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:3I6D"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:3I6D"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 263..273
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:3I6D"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 307..320
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 380..391
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 402..415
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 420..434
FT /evidence="ECO:0007829|PDB:3I6D"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:3I6D"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:3I6D"
FT HELIX 450..468
FT /evidence="ECO:0007829|PDB:3I6D"
SQ SEQUENCE 470 AA; 51203 MW; 95CC4E5847686D2E CRC64;
MSDGKKHVVI IGGGITGLAA AFYMEKEIKE KNLPLELTLV EASPRVGGKI QTVKKDGYII
ERGPDSFLER KKSAPQLVKD LGLEHLLVNN ATGQSYVLVN RTLHPMPKGA VMGIPTKIAP
FVSTGLFSLS GKARAAMDFI LPASKTKDDQ SLGEFFRRRV GDEVVENLIE PLLSGIYAGD
IDKLSLMSTF PQFYQTEQKH RSLILGMKKT RPQGSGQQLT AKKQGQFQTL STGLQTLVEE
IEKQLKLTKV YKGTKVTKLS HSGSCYSLEL DNGVTLDADS VIVTAPHKAA AGMLSELPAI
SHLKNMHSTS VANVALGFPE GSVQMEHEGT GFVISRNSDF AITACTWTNK KWPHAAPEGK
TLLRAYVGKA GDESIVDLSD NDIINIVLED LKKVMNINGE PEMTCVTRWH ESMPQYHVGH
KQRIKELREA LASAYPGVYM TGASFEGVGI PDCIDQGKAA VSDALTYLFS
