ARO1_ASPOR
ID ARO1_ASPOR Reviewed; 1595 AA.
AC Q2UCP6;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Pentafunctional AROM polypeptide {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=DHQS {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_03143};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=SK {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=Shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_03143};
GN Name=aroM {ECO:0000255|HAMAP-Rule:MF_03143}; ORFNames=AO090012000502;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
CC reactions in prechorismate polyaromatic amino acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03143};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
CC Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
CC EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03143};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate
CC cyclases superfamily. Dehydroquinate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase
CC family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_03143}.
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DR EMBL; AP007161; BAE60669.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UCP6; -.
DR SMR; Q2UCP6; -.
DR STRING; 510516.Q2UCP6; -.
DR EnsemblFungi; BAE60669; BAE60669; AO090012000502.
DR HOGENOM; CLU_001201_1_2_1; -.
DR OMA; YCYDDHR; -.
DR UniPathway; UPA00053; UER00085.
DR UniPathway; UPA00053; UER00086.
DR UniPathway; UPA00053; UER00087.
DR UniPathway; UPA00053; UER00088.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00502; DHQase_I; 1.
DR CDD; cd01556; EPSP_synthase; 1.
DR CDD; cd00464; SK; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.65.10.10; -; 2.
DR HAMAP; MF_00210; EPSP_synth; 1.
DR HAMAP; MF_03143; Pentafunct_AroM; 1.
DR HAMAP; MF_00109; Shikimate_kinase; 1.
DR InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030960; DHQS/DOIS.
DR InterPro; IPR001381; DHquinase_I.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR InterPro; IPR006264; EPSP_synthase.
DR InterPro; IPR023193; EPSP_synthase_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008289; Pentafunct_AroM.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR010110; Shikimate_DH_AroM-type.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR InterPro; IPR023000; Shikimate_kinase_CS.
DR Pfam; PF01761; DHQ_synthase; 1.
DR Pfam; PF01487; DHquinase_I; 1.
DR Pfam; PF00275; EPSP_synthase; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR Pfam; PF01202; SKI; 1.
DR PIRSF; PIRSF000514; Pentafunct_AroM; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR01356; aroA; 1.
DR TIGRFAMs; TIGR01357; aroB; 1.
DR TIGRFAMs; TIGR01093; aroD; 1.
DR TIGRFAMs; TIGR01809; Shik-DH-AROM; 1.
DR PROSITE; PS01028; DEHYDROQUINASE_I; 1.
DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
DR PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW Cytoplasm; Kinase; Lyase; Metal-binding; Multifunctional enzyme; NADP;
KW Nucleotide-binding; Oxidoreductase; Reference proteome; Transferase; Zinc.
FT CHAIN 1..1595
FT /note="Pentafunctional AROM polypeptide"
FT /id="PRO_0000406707"
FT REGION 1..384
FT /note="3-dehydroquinate synthase"
FT REGION 397..842
FT /note="EPSP synthase"
FT REGION 864..1055
FT /note="Shikimate kinase"
FT REGION 1056..1276
FT /note="3-dehydroquinase"
FT REGION 1289..1595
FT /note="Shikimate dehydrogenase"
FT ACT_SITE 260
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 275
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 824
FT /note="For EPSP synthase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1179
FT /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1207
FT /note="Schiff-base intermediate with substrate; for 3-
FT dehydroquinate dehydratase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 44..46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 81..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 114..116
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 130
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 139..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 146
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 152
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 162
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 179..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 194..197
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 250
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 264..268
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 271
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 287
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 356
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 871..878
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
SQ SEQUENCE 1595 AA; 173486 MW; 57BD3EC904C8C0D7 CRC64;
MAEPTKIKIL GQESIIADFG LWRNYVAKDL ISGCPSTTYV LITDTNIGSI YTPGFQKTFE
DAATAVSPAP RLLVYHCPPG EVSKSRQTKA DIEDWMLSQS PPCGRDTVVI ALGGGVIGDL
TGFVASTYMR GVRYVQVPTT LLAMVDSSIG GKTAIDTPLG KNLIGAIWQP TRIYIDLEFL
ETLPVREFVN GMAEVIKTAA ISSEEEFTAL EDNAEAILTA VRSERKPGQR WFEGIEDILK
ARILASARHK AYVVSADERE GGLRNLLNWG HSIGHAIEAI LTPQVLHGEC VAIGMVKEAE
LARHLGILKG VAVARIVKCI AAYGLPTSLK DSRIRKLTAG KHCSVDQLLF NMALDKKNDG
PKKKIVLLSA IGRTYEPKAS VVPNEDIGVV LAPSIEVHPG VEPASNIICI PPGSKSISNR
ALVLAALGSG TCRVKNLLHS DDTEVMLNAL ERLGAATFSW EEEGEVLVVN GKGGNLQASP
SELYLGNAGT ASRFLTTVAT LANASSVDSS ILTGNNRMKQ RPIGDLVDAL TANGASVEYV
ERKGSLPLKV AASGGFAGGR INLAAKVSSQ YVSSLLMCAP YAKEPVTLKL VGGKPISQPY
IDMTTAMMRS FGIDVQKSTT EEHTYHIPQG RYVNPAEYVI ESDASSATYP LAIAAITGTT
CTVPNIGSKS LQGDARFAVE VLGPMGCTVK QTDTSTTVVG PSDGILRPLP NVDMEPMTDA
FLTASVLAAV ARGDGASHTT RIYGIANQRV KECNRIKAMK DELAKFGVVC REHDDGLEID
GIDRSTLRQP AGGVYCYDDH RVAFSFSVLS LVAPQPTLIL EKECVGKTWP GWWDTLRQKF
SAKLEGKELK EEESSPLAGA GRATASVFII GMRGAGKTTT GRWVAKTLNR PFVDLDTELE
NVEGQTIPDI VKQRGWQGFR DAELSLLQRT LKERSSGYVL ACGGGIVEIP EARKLLIDYH
KNKGNVMLIM RDIKQVMDFL NIDKTRPAYV EDMMGVWLRR KPWFQECSNI QYYSQHATGK
LAKASEDFTR FFNVVTGEAD SLSIIKRKKH SFFVSLTLPD LRTAGDILEK VCVGSDAVEL
RVDLLKDPAS DSDIPSVDYV AEQMAFLRSY VSLPLIFTIR TKSQGGRFPD DAHDAAMELY
RLAFRSGSEF VDLEIAFPDE MLRAVTEMKG YSKIIASHHD PKGELSWANM SWMKYYNRAL
EYGDIIKLVG VAKNLDDNTA LRKFKSWAEE AHETPLIAIN MGDNGQLSRI LNGFMTPVSH
PSLPFKAAPG QLSATEIRKG LSLMGEIKQK KFAVFGTPVS GSRSPVLHNT LFSQAGLPHE
YGRLETANVE DVKDFIRSPD FGGASVTIPL KLDIMPLLDH ITPEAEIIGA VNTIIPVADG
DKPARLVGSN TDWQGMTLSL HNAGVETANK DASALVIGGG GTARAAIYAL HSMGFSPIYV
IGRSAPKLQS MVSTFPSSYN IQVIDSPETL KTIPTVAIGT IPADKPIDPV MRETLCHMFE
RAQEADADVV KTGEKAHRVL LEMAYKPSVT ALMQLASDSN WHTIPGLEVL VGQGWYQVSS
KPYTYSIQYQ KLTRYIVQTL DWDFSPLRGC KSRRA
