METE_CANAL
ID METE_CANAL Reviewed; 767 AA.
AC P82610; A0A1D8PS13; Q5A9B4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000303|PubMed:21689631, ECO:0000303|PubMed:24524835, ECO:0000303|PubMed:25545590};
DE EC=2.1.1.14 {ECO:0000269|PubMed:21689631, ECO:0000269|PubMed:24524835, ECO:0000269|PubMed:25545590};
DE AltName: Full=Cobalamin-independent methionine synthase {ECO:0000303|PubMed:21689631, ECO:0000303|PubMed:24524835, ECO:0000303|PubMed:25545590};
DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme;
GN Name=MET6 {ECO:0000303|PubMed:21689631, ECO:0000303|PubMed:24524835};
GN OrderedLocusNames=CAALFM_CR01620CA; ORFNames=CaO19.10083, CaO19.2551;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PROTEIN SEQUENCE OF 2-15.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=11681208;
RX DOI=10.1002/1615-9861(200104)1:4<550::aid-prot550>3.0.co;2-w;
RA Pitarch A., Diez-Orejas R., Molero G., Pardo M., Sanchez M., Gil C.,
RA Nombela C.;
RT "Analysis of the serologic response to systemic Candida albicans infection
RT in a murine model.";
RL Proteomics 1:550-559(2001).
RN [5]
RP PROTEIN SEQUENCE OF 411-421, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=10949142;
RX DOI=10.1002/1522-2683(20000701)21:13<2651::aid-elps2651>3.0.co;2-3;
RA Pardo M., Ward M., Pitarch A., Sanchez M., Nombela C., Blackstock W.,
RA Gil C.;
RT "Cross-species identification of novel Candida albicans immunogenic
RT proteins by combination of two-dimensional polyacrylamide gel
RT electrophoresis and mass spectrometry.";
RL Electrophoresis 21:2651-2659(2000).
RN [6] {ECO:0007744|PDB:3PPC, ECO:0007744|PDB:3PPF, ECO:0007744|PDB:3PPG, ECO:0007744|PDB:3PPH}
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF MUTANTS ALA-103/ALA-104/ALA-107;
RP THR-103/THR-104/THR-107 AND TYR-103/TYR-104/TYR-107 AND IN COMPLEXES WITH
RP ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND MUTAGENESIS OF
RP LYS-103; LYS-104 AND GLU-107.
RX PubMed=21689631; DOI=10.1016/j.abb.2011.06.002;
RA Ubhi D., Kavanagh K.L., Monzingo A.F., Robertus J.D.;
RT "Structure of Candida albicans methionine synthase determined by employing
RT surface residue mutagenesis.";
RL Arch. Biochem. Biophys. 513:19-26(2011).
RN [7] {ECO:0007744|PDB:4L5Z, ECO:0007744|PDB:4L61, ECO:0007744|PDB:4L64, ECO:0007744|PDB:4L65, ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4L6O}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEXES WITH
RP 5-METHYLTETRAHYDROFOLATEGLUTAMATE; L-HOMOCYSTEINE; L-METHIONINE;
RP METHOTREXATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP MUTAGENESIS OF ASN-126 AND TYR-660.
RX PubMed=24524835; DOI=10.1016/j.jmb.2014.02.006;
RA Ubhi D., Kago G., Monzingo A.F., Robertus J.D.;
RT "Structural analysis of a fungal methionine synthase with substrates and
RT inhibitors.";
RL J. Mol. Biol. 426:1839-1847(2014).
RN [8] {ECO:0007744|PDB:4QQU}
RP X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) IN COMPLEX WITH
RP 5-METHYLTETRAHYDROFOLATEGLUTAMATE; L-HOMOCYSTEINE AND ZINC, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, PATHWAY, ACTIVE SITE, REACTION MECHANISM, AND
RP MUTAGENESIS OF MET-119; LYS-121; HIS-128; GLN-451; ARG-456; ARG-459 AND
RP HIS-707.
RX PubMed=25545590; DOI=10.1016/j.jmb.2014.12.014;
RA Ubhi D.K., Robertus J.D.;
RT "The cobalamin-independent methionine synthase enzyme captured in a
RT substrate-induced closed conformation.";
RL J. Mol. Biol. 427:901-909(2015).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC methyltetrahydrofolate to homocysteine resulting in methionine
CC formation. {ECO:0000269|PubMed:21689631, ECO:0000269|PubMed:24524835,
CC ECO:0000269|PubMed:25545590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-
CC methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199,
CC ChEBI:CHEBI:58207; EC=2.1.1.14;
CC Evidence={ECO:0000269|PubMed:21689631, ECO:0000269|PubMed:24524835,
CC ECO:0000269|PubMed:25545590};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21689631, ECO:0000269|PubMed:24524835,
CC ECO:0000269|PubMed:25545590};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:21689631,
CC ECO:0000269|PubMed:24524835, ECO:0000269|PubMed:25545590};
CC -!- ACTIVITY REGULATION: Inhibited weakly by methotrexate.
CC {ECO:0000269|PubMed:24524835}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for homocysteine (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:24524835};
CC KM=87 uM for 5-methyltetrahydrofolate-triglutamate (at 37 degrees
CC Celsius {ECO:0000269|PubMed:24524835};
CC Note=kcat is 25 min(-1) for homocysteine. kcat is 29 min(-1) for 5-
CC methyl-tetrahydrofolate-triglutamate. {ECO:0000269|PubMed:24524835};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC {ECO:0000269|PubMed:21689631, ECO:0000269|PubMed:24524835,
CC ECO:0000269|PubMed:25545590}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {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; CP017630; AOW30921.1; -; Genomic_DNA.
DR RefSeq; XP_718219.1; XM_713126.2.
DR PDB; 3PPC; X-ray; 2.20 A; A/B=1-767.
DR PDB; 3PPF; X-ray; 2.30 A; A=1-767.
DR PDB; 3PPG; X-ray; 1.98 A; A=1-767.
DR PDB; 3PPH; X-ray; 2.80 A; A/B=1-767.
DR PDB; 4L5Z; X-ray; 2.18 A; A=1-767.
DR PDB; 4L61; X-ray; 2.13 A; A=1-767.
DR PDB; 4L64; X-ray; 2.18 A; A=1-767.
DR PDB; 4L65; X-ray; 2.31 A; A=1-767.
DR PDB; 4L6H; X-ray; 1.75 A; A=1-767.
DR PDB; 4L6O; X-ray; 1.88 A; A=1-767.
DR PDB; 4QQU; X-ray; 2.98 A; A=1-767.
DR PDBsum; 3PPC; -.
DR PDBsum; 3PPF; -.
DR PDBsum; 3PPG; -.
DR PDBsum; 3PPH; -.
DR PDBsum; 4L5Z; -.
DR PDBsum; 4L61; -.
DR PDBsum; 4L64; -.
DR PDBsum; 4L65; -.
DR PDBsum; 4L6H; -.
DR PDBsum; 4L6O; -.
DR PDBsum; 4QQU; -.
DR AlphaFoldDB; P82610; -.
DR SMR; P82610; -.
DR BioGRID; 1223094; 1.
DR STRING; 237561.P82610; -.
DR COMPLUYEAST-2DPAGE; P82610; -.
DR PRIDE; P82610; -.
DR GeneID; 3640084; -.
DR KEGG; cal:CAALFM_CR01620CA; -.
DR CGD; CAL0000186137; MET6.
DR VEuPathDB; FungiDB:CR_01620C_A; -.
DR eggNOG; KOG2263; Eukaryota.
DR HOGENOM; CLU_013175_0_0_1; -.
DR InParanoid; P82610; -.
DR OMA; KVMKGML; -.
DR OrthoDB; 237390at2759; -.
DR BRENDA; 2.1.1.14; 1096.
DR UniPathway; UPA00051; UER00082.
DR EvolutionaryTrace; P82610; -.
DR PRO; PR:P82610; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IDA:CGD.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046084; P:adenine biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0034605; P:cellular response to heat; IEP:CGD.
DR GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
DR GO; GO:0019280; P:L-methionine biosynthetic process from homoserine via O-acetyl-L-homoserine and cystathionine; IEA:EnsemblFungi.
DR GO; GO:0009086; P:methionine biosynthetic process; IMP:CGD.
DR GO; GO:0006555; P:methionine metabolic process; IDA:CGD.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd03311; CIMS_C_terminal_like; 1.
DR Gene3D; 3.20.20.210; -; 2.
DR HAMAP; MF_00172; Meth_synth; 1.
DR InterPro; IPR013215; Cbl-indep_Met_Synth_N.
DR InterPro; IPR006276; Cobalamin-indep_Met_synthase.
DR InterPro; IPR002629; Met_Synth_C/arc.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR Pfam; PF08267; Meth_synt_1; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR SUPFAM; SSF51726; SSF51726; 2.
DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Direct protein sequencing;
KW Metal-binding; Methionine biosynthesis; Methyltransferase;
KW Reference proteome; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11681208"
FT CHAIN 2..767
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000098702"
FT ACT_SITE 707
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:25545590"
FT BINDING 19
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L64,
FT ECO:0007744|PDB:4L65, ECO:0007744|PDB:4L6H,
FT ECO:0007744|PDB:4QQU"
FT BINDING 126
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L65,
FT ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4QQU"
FT BINDING 446..448
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L5Z,
FT ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4QQU"
FT BINDING 446..448
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0007744|PDB:4L61, ECO:0007744|PDB:4L65"
FT BINDING 499
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L5Z,
FT ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4QQU"
FT BINDING 499
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0007744|PDB:4L61, ECO:0007744|PDB:4L65"
FT BINDING 504
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L65,
FT ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4QQU"
FT BINDING 527
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L64,
FT ECO:0007744|PDB:4L65, ECO:0007744|PDB:4L6H,
FT ECO:0007744|PDB:4QQU"
FT BINDING 530..531
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L64,
FT ECO:0007744|PDB:4L65, ECO:0007744|PDB:4QQU"
FT BINDING 576
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L64,
FT ECO:0007744|PDB:4L65, ECO:0007744|PDB:4L6H,
FT ECO:0007744|PDB:4QQU"
FT BINDING 614
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L5Z,
FT ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4QQU"
FT BINDING 614
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:24524835,
FT ECO:0007744|PDB:4L61, ECO:0007744|PDB:4L65"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21689631,
FT ECO:0000269|PubMed:24524835, ECO:0000269|PubMed:25545590,
FT ECO:0007744|PDB:3PPC, ECO:0007744|PDB:3PPG,
FT ECO:0007744|PDB:4L5Z, ECO:0007744|PDB:4L61,
FT ECO:0007744|PDB:4L64, ECO:0007744|PDB:4L65,
FT ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4L6O,
FT ECO:0007744|PDB:4QQU"
FT BINDING 659
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21689631,
FT ECO:0000269|PubMed:24524835, ECO:0000269|PubMed:25545590,
FT ECO:0007744|PDB:3PPC, ECO:0007744|PDB:3PPG,
FT ECO:0007744|PDB:4L5Z, ECO:0007744|PDB:4L61,
FT ECO:0007744|PDB:4L64, ECO:0007744|PDB:4L65,
FT ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4L6O,
FT ECO:0007744|PDB:4QQU"
FT BINDING 679
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21689631,
FT ECO:0000269|PubMed:24524835, ECO:0007744|PDB:3PPG,
FT ECO:0007744|PDB:4L61, ECO:0007744|PDB:4L64,
FT ECO:0007744|PDB:4L6O"
FT BINDING 739
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21689631,
FT ECO:0000269|PubMed:24524835, ECO:0000269|PubMed:25545590,
FT ECO:0007744|PDB:3PPC, ECO:0007744|PDB:3PPG,
FT ECO:0007744|PDB:4L5Z, ECO:0007744|PDB:4L61,
FT ECO:0007744|PDB:4L64, ECO:0007744|PDB:4L65,
FT ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4L6O,
FT ECO:0007744|PDB:4QQU"
FT MUTAGEN 103
FT /note="K->Y,A,T: No effect on catalytic activity; when
FT associated with A-104 and A-107, or with T-104 and T-107,
FT or with Y-104 and Y-107."
FT /evidence="ECO:0000269|PubMed:21689631"
FT MUTAGEN 104
FT /note="K->Y,A,T: No effect on catalytic activity; when
FT associated with A-103 and A-107, or with T-103 and T-107,
FT or with Y-103 and Y-107."
FT /evidence="ECO:0000269|PubMed:21689631"
FT MUTAGEN 107
FT /note="E->Y,A,T: No effect on catalytic activity; when
FT associated with A-103 and A-104, or with T-103 and T-104,
FT or with Y-103 and Y-104."
FT /evidence="ECO:0000269|PubMed:21689631"
FT MUTAGEN 119
FT /note="M->A: 22% of the catalytic activity of the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:25545590"
FT MUTAGEN 121
FT /note="K->A: Less than 5% of the catalytic activity of the
FT wild-type."
FT /evidence="ECO:0000269|PubMed:25545590"
FT MUTAGEN 126
FT /note="N->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24524835"
FT MUTAGEN 128
FT /note="H->A: 26% of the catalytic activity of the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:25545590"
FT MUTAGEN 451
FT /note="Q->A: Less than 5% of the catalytic activity of the
FT wild-type."
FT /evidence="ECO:0000269|PubMed:25545590"
FT MUTAGEN 456
FT /note="R->A: 38% of the catalytic activity of the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:25545590"
FT MUTAGEN 459
FT /note="R->A: Less than 5% of the catalytic activity of the
FT wild-type."
FT /evidence="ECO:0000269|PubMed:25545590"
FT MUTAGEN 660
FT /note="Y->A,Q: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24524835"
FT MUTAGEN 660
FT /note="Y->F: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:24524835"
FT MUTAGEN 707
FT /note="H->A,K: Less than 5% of the catalytic activity of
FT the wild-type."
FT /evidence="ECO:0000269|PubMed:25545590"
FT CONFLICT 5
FT /note="S -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:4L5Z"
FT HELIX 32..53
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3PPH"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3PPC"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 193..210
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:4L6H"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 312..326
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 363..377
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 383..398
FT /evidence="ECO:0007829|PDB:4L6H"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 425..436
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 453..463
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 469..489
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 513..517
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 536..542
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 570..575
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 585..605
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 610..614
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 618..621
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 624..627
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 628..645
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:3PPG"
FT STRAND 652..658
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:3PPC"
FT HELIX 665..671
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 674..678
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:3PPH"
FT HELIX 686..690
FT /evidence="ECO:0007829|PDB:4L6H"
FT TURN 691..694
FT /evidence="ECO:0007829|PDB:4L61"
FT STRAND 697..701
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:4L61"
FT HELIX 714..725
FT /evidence="ECO:0007829|PDB:4L6H"
FT HELIX 730..732
FT /evidence="ECO:0007829|PDB:4L6H"
FT STRAND 733..735
FT /evidence="ECO:0007829|PDB:4L6H"
FT TURN 740..743
FT /evidence="ECO:0007829|PDB:3PPH"
FT HELIX 746..766
FT /evidence="ECO:0007829|PDB:4L6H"
SQ SEQUENCE 767 AA; 85702 MW; 21BE228C99259471 CRC64;
MVQSSVLGFP RIGGQRELKK ITEAYWSGKA TVEELLAKGK ELREHNWKLQ QKAGVDIIPS
NDFSYYDQVL DLSLLFNAIP ERYTKFDLAP IDVLFAMGRG LQKKATETQA AVDVTALEMV
KWFDSNYHYV RPTFSHSTEF KLNTAAGIKP VDEFNEAKAL GVQTRPVILG PVSYLYLGKA
DKDSLDLEPI SLLPKILPVY KELLQKLKEA GAEQVQIDEP VLVLDLPEAV QSKFKEAYDA
LVGADVPELI LTTYFGDVRP NLKAIENLPV AGFHFDFVRV PEQLDEVASI LKDGQTLSAG
VVDGRNIWKT DFAKASAVVQ KAIEKVGKDK VVVATSSSLL HTPVDLESET KLDAVIKDWF
SFATQKLDEV VVIAKNVSGE DVSKQLEANA ASIKARSESS ITNDPKVQER LTTINEALAT
RKAAFPERLT EQKAKYNLPL FPTTTIGSFP QTKDIRINRN KFAKGQITAE EYEAFINKEI
ETVVRFQEEI GLDVLVHGEP ERNDMVQYFG EQLNGFAFTT NGWVQSYGSR YVRPPIIVGD
VSRPKAMTVK ESVYAQSITS KPMKGMLTGP VTILRWSFPR DDVSGKIQAL QLGLALRDEV
NDLEGAGITV IQVDEPAIRE GLPLRAGKER SDYLNWAAQS FRVATSGVEN STQIHSHFCY
SDLDPNHIKA LDADVVSIEF SKKDDPNYIQ EFSEYPNHIG LGLFDIHSPR IPSKQEFVSR
IEEILKVYPA SKFWVNPDCG LKTRGWPEVK ESLTNMVEAA KEFRAKY
