RBL1_HALNC
ID RBL1_HALNC Reviewed; 473 AA.
AC O85040; D0KZ92;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:18258595};
DE AltName: Full=Form 1 RuBisCO {ECO:0000303|PubMed:9696760};
GN Name=cbbL {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000303|PubMed:9696760};
GN OrderedLocusNames=Hneap_0922;
OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS neapolitanus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Halothiobacillaceae; Halothiobacillus.
OX NCBI_TaxID=555778;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=9696760; DOI=10.1128/jb.180.16.4133-4139.1998;
RA Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.;
RT "Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate
RT carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in
RT expression of form II RuBisCO, loss of carboxysomes, and an increased CO2
RT requirement for growth.";
RL J. Bacteriol. 180:4133-4139(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Kerfeld C., Cannon G., Heinhort S.;
RT "Complete sequence of Halothiobacillus neapolitanus c2.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX DOI=10.1007/BF00429407;
RA Cannon G.C., Shively J.M.;
RT "Characterization of a Homogenous Preparation of Carboxysomes from
RT Thiobacillus neapolitanus.";
RL Arch. Microbiol. 134:52-59(1983).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16535117; DOI=10.1128/aem.61.9.3256-3260.1995;
RA English R.S., Jin S., Shively J.M.;
RT "Use of Electroporation To Generate a Thiobacillus neapolitanus Carboxysome
RT Mutant.";
RL Appl. Environ. Microbiol. 61:3256-3260(1995).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=14729686; DOI=10.1128/jb.186.3.623-630.2004;
RA So A.K., Espie G.S., Williams E.B., Shively J.M., Heinhorst S.,
RA Cannon G.C.;
RT "A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a
RT component of the carboxysome shell.";
RL J. Bacteriol. 186:623-630(2004).
RN [6]
RP PROTEIN ABUNDANCE, AND SUBCELLULAR LOCATION.
RX DOI=10.1007/7171_023;
RA Heinhorst S., Cannon G.C., Shively J.M.;
RT "Carboxysomes and Carboxysome-like Inclusions.";
RL (In) Shively J.M. (eds.);
RL Microbiology Monographs, pp.2:141-164, Springer-Verlag, Berlin (2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=18258595; DOI=10.1074/jbc.m709285200;
RA Dou Z., Heinhorst S., Williams E.B., Murin C.D., Shively J.M., Cannon G.C.;
RT "CO2 fixation kinetics of Halothiobacillus neapolitanus mutant carboxysomes
RT lacking carbonic anhydrase suggest the shell acts as a diffusional barrier
RT for CO2.";
RL J. Biol. Chem. 283:10377-10384(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, CARBOXYSOME ASSEMBLY PROCESS, REQUIRED FOR
RP CARBOXYSOMAL TARGETING, DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=18974784; DOI=10.1371/journal.pone.0003570;
RA Menon B.B., Dou Z., Heinhorst S., Shively J.M., Cannon G.C.;
RT "Halothiobacillus neapolitanus carboxysomes sequester heterologous and
RT chimeric RubisCO species.";
RL PLoS ONE 3:e3570-e3570(2008).
RN [9]
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=22184212; DOI=10.1073/pnas.1108557109;
RA Bonacci W., Teng P.K., Afonso B., Niederholtmeyer H., Grob P., Silver P.A.,
RA Savage D.F.;
RT "Modularity of a carbon-fixing protein organelle.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:478-483(2012).
RN [10]
RP SUBUNIT.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=25826651; DOI=10.3390/life5021141;
RA Cai F., Dou Z., Bernstein S.L., Leverenz R., Williams E.B., Heinhorst S.,
RA Shively J., Cannon G.C., Kerfeld C.A.;
RT "Advances in Understanding Carboxysome Assembly in Prochlorococcus and
RT Synechococcus Implicate CsoS2 as a Critical Component.";
RL Life 5:1141-1171(2015).
RN [11]
RP BIOTECHNOLOGY.
RX PubMed=29922315; DOI=10.3389/fpls.2018.00739;
RA Fang Y., Huang F., Faulkner M., Jiang Q., Dykes G.F., Yang M., Liu L.N.;
RT "Engineering and Modulating Functional Cyanobacterial CO2-Fixing
RT Organelles.";
RL Front. Plant Sci. 9:739-739(2018).
RN [12]
RP INTERACTION WITH CSOS1A; CSOS1B AND CSOS1C, DOMAIN, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=30305640; DOI=10.1038/s41598-018-33074-x;
RA Liu Y., He X., Lim W., Mueller J., Lawrie J., Kramer L., Guo J., Niu W.;
RT "Deciphering molecular details in the assembly of alpha-type carboxysome.";
RL Sci. Rep. 8:15062-15062(2018).
RN [13]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=31406332; DOI=10.1038/s41564-019-0520-8;
RA Desmarais J.J., Flamholz A.I., Blikstad C., Dugan E.J., Laughlin T.G.,
RA Oltrogge L.M., Chen A.W., Wetmore K., Diamond S., Wang J.Y., Savage D.F.;
RT "DABs are inorganic carbon pumps found throughout prokaryotic phyla.";
RL Nat. Microbiol. 4:2204-2215(2019).
RN [14] {ECO:0007744|PDB:1SVD}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RA Kerfeld C.A., Sawaya M.R., Pashkov I., Cannon G., Williams E., Tran K.,
RA Yeates T.O.;
RT "The structure of Halothiobacillus neapolitanus Rubisco.";
RL Submitted (APR-2005) to the PDB data bank.
RN [15] {ECO:0007744|PDB:6UEW}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF HOLOENZYME, INTERACTION WITH
RP CSOS2, AND MUTAGENESIS OF TYR-72 AND PHE-346.
RX PubMed=32123388; DOI=10.1038/s41594-020-0387-7;
RA Oltrogge L.M., Chaijarasphong T., Chen A.W., Bolin E.R., Marqusee S.,
RA Savage D.F.;
RT "Multivalent interactions between CsoS2 and Rubisco mediate alpha-
RT carboxysome formation.";
RL Nat. Struct. Mol. Biol. 27:281-287(2020).
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate. Both reactions occur simultaneously and in competition at
CC the same active site (By similarity) (Ref.3, PubMed:18258595,
CC PubMed:18974784). There are estimated to be 270 RuBisCO
CC heterohexadecamers per carboxysome (Ref.6). {ECO:0000255|HAMAP-
CC Rule:MF_01338, ECO:0000269|PubMed:18258595,
CC ECO:0000269|PubMed:18974784, ECO:0000269|Ref.3, ECO:0000269|Ref.6}.
CC -!- FUNCTION: Alpha-carboxysomes are able to assemble in the absence of
CC RuBisCO, unlike beta-carboxysomes. The RuBisCO large subunit is
CC required for enzyme integration into carboxysomes; replacing it with
CC the carboxysomally targeted gene (Tcr_0838, AC Q31HD9) of H.crungenus
CC places RuBisCO in the carboxysome, while the non-carboxysomal large
CC subunit of H.crungenus (Tcr_0427, AC Q31IK0) is not incorporated in the
CC carboxysome. {ECO:0000269|PubMed:18974784}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01338, ECO:0000269|PubMed:18258595,
CC ECO:0000269|PubMed:18974784, ECO:0000269|Ref.3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338,
CC ECO:0000269|Ref.3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=163.7 uM for CO(2);
CC Vmax=2.9 umol/min/mg enzyme {ECO:0000269|PubMed:18258595};
CC Note=For enzyme freed from the carboxysome.
CC {ECO:0000269|PubMed:18258595};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains (By
CC similarity) (Ref.14). Forms a CsoS2-CsoS1-RuBisCO complex (Probable).
CC The N-terminus (residues 1-136) interacts with shell proteins CsoS1A,
CC CsoS1B and CsoS1C (PubMed:30305640). Holo-RuBisCO interacts with the N-
CC terminal repeats of CsoS2; binding is sensitive to ionic strength. A
CC fusion of a single N-terminal repeat to the C-terminus of the large
CC subunit of RuBisCO (cbbL) shows the repeat can lie between a CbbL
CC dimer, making minor contacts to CbbS; thus each RuBisCO holoenzyme
CC could bind 8 repeats (PubMed:32123388). {ECO:0000255|HAMAP-
CC Rule:MF_01338, ECO:0000269|PubMed:30305640,
CC ECO:0000269|PubMed:32123388, ECO:0000269|Ref.14,
CC ECO:0000305|PubMed:25826651}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:14729686,
CC ECO:0000269|PubMed:18974784, ECO:0000269|Ref.3,
CC ECO:0000305|PubMed:16535117}. Note=When the major carboxysomal shell
CC protein CsoS1A is disrupted most RuBisCO is found in the soluble
CC (cytoplasmic) fraction (PubMed:16535117). Most protein is found in the
CC carboxysome interior and not associated with the shell
CC (PubMed:14729686). This bacterium makes alpha-type carboxysomes (Ref.6,
CC PubMed:18258595). {ECO:0000269|PubMed:14729686,
CC ECO:0000269|PubMed:16535117, ECO:0000269|PubMed:18258595,
CC ECO:0000269|Ref.6}.
CC -!- INDUCTION: Produced when grown in air or in air supplemented with 5%
CC CO(2) (at protein level). Part of the cbbL-cbbS operon.
CC {ECO:0000269|PubMed:9696760}.
CC -!- DOMAIN: The N-terminus (minimally 1-122, fragment 1-136 does not bind
CC any better) interacts with the shell proteins CsoS1A, CsoS1B and
CC CsoS1C. A slightly longer fragment of the N-terminus (residues 1-136)
CC is required for targeting to carboxysomes, and will direct foreign
CC proteins to the carboxysome, with reduced efficiency compared to the
CC whole protein. {ECO:0000269|PubMed:30305640}.
CC -!- DISRUPTION PHENOTYPE: Does not grow in air, grows poorly in air
CC supplemented with 5% CO(2), a high-CO(2) requiring phenotype (hcr), has
CC apolar effect on expression of downstream cbbS. Expresses type II but
CC not type I RuBisCO, does not form carboxysomes but instead smaller,
CC empty cytoplasmic inclusions (PubMed:9696760). A double ccbL-ccbS
CC deletion is hcr and forms empty but otherwise normal appearing
CC carboxysomes (PubMed:18974784). Required for growth in ambient air
CC (PubMed:31406332). {ECO:0000269|PubMed:18974784,
CC ECO:0000269|PubMed:31406332, ECO:0000269|PubMed:9696760}.
CC -!- BIOTECHNOLOGY: Expression of 10 genes for alpha-carboxysome (Cb)
CC proteins (cbbL-cbbS-csoS2-csoS3-csoS4A-csoS4B-csoS1C-csoS1A-csoS1B-
CC csoS1D) in E.coli generates compartments that resemble Cb, contain
CC RuBisCO and have its catalytic activity, showing it is possible to make
CC artificial, functional Cb using these 10 genes. Cargo proteins can be
CC targeted to these organelles (PubMed:22184212, PubMed:30305640). Alpha-
CC carboxysomes are assembled in the complete absence of this enzyme in
CC this bacteria, suggesting carboxysome-based microcompartments can be
CC designed for applications such as custom chemical reactors or delivery
CC vehicles (PubMed:18974784). When this gene is expressed in S.elongatus
CC PCC 7942 it colocalizes with its beta-carboxysomes, suggesting there a
CC range of modular possibilites for the carboxysome constituent proteins.
CC These experiments open the door to generating carboxysomes in plant
CC cells to increase their photosynthesis and productivity, as well as
CC tailoring bacterial microcompartments to specific metabolic needs and
CC molecule delivery (PubMed:29922315). {ECO:0000269|PubMed:18974784,
CC ECO:0000269|PubMed:22184212, ECO:0000269|PubMed:29922315,
CC ECO:0000269|PubMed:30305640}.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR EMBL; AF038430; AAC32549.1; -; Genomic_DNA.
DR EMBL; CP001801; ACX95765.1; -; Genomic_DNA.
DR RefSeq; WP_012823801.1; NC_013422.1.
DR PDB; 1SVD; X-ray; 1.80 A; A=1-473.
DR PDB; 6UEW; X-ray; 2.40 A; A/C/E/G=2-473.
DR PDBsum; 1SVD; -.
DR PDBsum; 6UEW; -.
DR AlphaFoldDB; O85040; -.
DR SMR; O85040; -.
DR STRING; 555778.Hneap_0922; -.
DR PRIDE; O85040; -.
DR EnsemblBacteria; ACX95765; ACX95765; Hneap_0922.
DR KEGG; hna:Hneap_0922; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_2_0_6; -.
DR OMA; EYRETYW; -.
DR OrthoDB; 848380at2; -.
DR BRENDA; 4.1.1.39; 6349.
DR EvolutionaryTrace; O85040; -.
DR Proteomes; UP000009102; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR HAMAP; MF_01338; RuBisCO_L_type1; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR InterPro; IPR020888; RuBisCO_lsuI.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Calvin cycle;
KW Carbon dioxide fixation; Carboxysome; Lyase; Magnesium; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..473
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062660"
FT REGION 1..136
FT /note="Necessary and sufficient to target proteins to
FT carboxysomes, interacts with shell proteins"
FT /evidence="ECO:0000269|PubMed:30305640"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 116
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 327
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 194
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MUTAGEN 72
FT /note="Y->A: No longer binds N-repeats in CsoS2A; when
FT associated with A-346 and 'A-96' in CbbS."
FT /evidence="ECO:0000269|PubMed:32123388"
FT MUTAGEN 72
FT /note="Y->R: No longer binds N-repeats in CsoS2A."
FT /evidence="ECO:0000269|PubMed:32123388"
FT MUTAGEN 346
FT /note="F->A: No longer binds N-repeats in CsoS2A; when
FT associated with A-72 and 'A-96' in CbbS."
FT /evidence="ECO:0000269|PubMed:32123388"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:6UEW"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:1SVD"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:1SVD"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 175..187
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 207..225
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:1SVD"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 333..343
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 380..387
FT /evidence="ECO:0007829|PDB:1SVD"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 406..425
FT /evidence="ECO:0007829|PDB:1SVD"
FT TURN 430..433
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 434..442
FT /evidence="ECO:0007829|PDB:1SVD"
FT HELIX 446..455
FT /evidence="ECO:0007829|PDB:1SVD"
SQ SEQUENCE 473 AA; 52636 MW; B84D2EDE46CAF7D8 CRC64;
MAVKKYSAGV KEYRQTYWMP EYTPLDSDIL ACFKITPQPG VDREEAAAAV AAESSTGTWT
TVWTDLLTDM DYYKGRAYRI EDVPGDDAAF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF
KAVRGLRLED VRFPLAYVKT CGGPPHGIQV ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR
AVYECLRGGL DFTKDDENIN SQPFMRWRDR FLFVQDATET AEAQTGERKG HYLNVTAPTP
EEMYKRAEFA KEIGAPIIMH DYITGGFTAN TGLAKWCQDN GVLLHIHRAM HAVIDRNPNH
GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFIPED RSRGIFFDQD
WGSMPGVFAV ASGGIHVWHM PALVNIFGDD SVLQFGGGTL GHPWGNAAGA AANRVALEAC
VEARNQGRDI EKEGKEILTA AAQHSPELKI AMETWKEIKF EFDTVDKLDT QNR
