ID RBL_SYNP6 Reviewed; 472 AA.
AC P00880;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 27-MAR-2024, entry version 170.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE Short=RuBisCO large subunit;
DE EC=4.1.1.39 {ECO:0000269|PubMed:7922027, ECO:0000269|PubMed:9882445};
GN Name=cbbL; Synonyms=rbcA, rbcL; OrderedLocusNames=syc0130_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6307620; DOI=10.1089/dna.1983.2.121;
RA Reichelt B.Y., Delaney S.F.;
RT "The nucleotide sequence for the large subunit of ribulose 1,5-bisphosphate
RT carboxylase from a unicellular cyanobacterium, Synechococcus PCC6301.";
RL DNA 2:121-129(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CARBOXYLATION AT LYS-198.
RX PubMed=16593333; DOI=10.1073/pnas.80.13.4050;
RA Shinozaki K., Yamada C., Takahata N., Sugiura M.;
RT "Molecular cloning and sequence analysis of the cyanobacterial gene for the
RT large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4050-4054(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shinozaki K., Sugiura M.;
RT "Genes for the large and small subunits of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase constitute a single operon in a cyanobacterium
RT Anacystis nidulans 6301.";
RL Mol. Gen. Genet. 200:27-32(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
RN [5]
RP PROTEIN SEQUENCE OF 333-342.
RX PubMed=8031129; DOI=10.1006/abbi.1994.1301;
RA Read B.A., Tabita F.R.;
RT "High substrate specificity factor ribulose bisphosphate
RT carboxylase/oxygenase from eukaryotic marine algae and properties of
RT recombinant cyanobacterial RubiSCO containing 'algal' residue
RT modifications.";
RL Arch. Biochem. Biophys. 312:210-218(1994).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9882445; DOI=10.1006/abbi.1998.0979;
RA Horken K.M., Tabita F.R.;
RT "Closely related form I ribulose bisphosphate carboxylase/oxygenase
RT molecules that possess different CO2/O2 substrate specificities.";
RL Arch. Biochem. Biophys. 361:183-194(1999).
RN [7]
RP RUBISCO FOLDING AND ASSEMBLY, AND SUBUNIT.
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17574029; DOI=10.1016/j.cell.2007.04.025;
RA Saschenbrecker S., Bracher A., Rao K.V., Rao B.V., Hartl F.U.,
RA Hayer-Hartl M.;
RT "Structure and function of RbcX, an assembly chaperone for hexadecameric
RT Rubisco.";
RL Cell 129:1189-1200(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 6-472 OF ACTIVATED HOLOENZYME IN
RP COMPLEX WITH TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM, SUBUNIT, AND
RP DISULFIDE BOND.
RX PubMed=8245022; DOI=10.1016/s0021-9258(19)74469-x;
RA Newman J., Gutteridge S.;
RT "The X-ray structure of Synechococcus ribulose-bisphosphate
RT carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution.";
RL J. Biol. Chem. 268:25876-25886(1993).
RN [9] {ECO:0007744|PDB:1RSC}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF INACTIVATED HOLOENZYME IN COMPLEX
RP WITH PRODUCT ANALOG, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=7922027; DOI=10.1016/s0969-2126(00)00050-2;
RA Newman J., Gutteridge S.;
RT "Structure of an effector-induced inactivated state of ribulose 1,5-
RT bisphosphate carboxylase/oxygenase: the binary complex between enzyme and
RT xylulose 1,5-bisphosphate.";
RL Structure 2:495-502(1994).
RN [10] {ECO:0007744|PDB:2WVW}
RP STRUCTURE BY ELECTRON MICROSCOPY (9.00 ANGSTROMS) IN COMPLEX WITH ANABAENA
RP RBCX2, RUBISCO FOLDING AND ASSEMBLY, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP 461-GLU--LEU-472; PHE-464 AND PHE-466.
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=20075914; DOI=10.1038/nature08651;
RA Liu C., Young A.L., Starling-Windhof A., Bracher A., Saschenbrecker S.,
RA Rao B.V., Rao K.V., Berninghausen O., Mielke T., Hartl F.U., Beckmann R.,
RA Hayer-Hartl M.;
RT "Coupled chaperone action in folding and assembly of hexadecameric
RT Rubisco.";
RL Nature 463:197-202(2010).
RN [11] {ECO:0007744|PDB:3RG6}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH ANABAENA RBCX2,
RP RUBISCO FOLDING AND ASSEMBLY, SUBUNIT, AND MUTAGENESIS OF GLU-49; ALA-53;
RP 67-TRP--LEU-71; GLU-106; ALA-126 AND ARG-212.
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=21765418; DOI=10.1038/nsmb.2090;
RA Bracher A., Starling-Windhof A., Hartl F.U., Hayer-Hartl M.;
RT "Crystal structure of a chaperone-bound assembly intermediate of form I
RT Rubisco.";
RL Nat. Struct. Mol. Biol. 18:875-880(2011).
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 in the photorespiration process. Both reactions occur
CC simultaneously and in competition at the same active site.
CC {ECO:0000269|PubMed:7922027, ECO:0000269|PubMed:9882445}.
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:0000269|PubMed:7922027,
CC ECO:0000269|PubMed:9882445};
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:0000269|PubMed:9882445};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8245022};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:8245022};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=39 uM for ribulose 1,5-bisphosphate {ECO:0000269|PubMed:9882445};
CC KM=173 uM for CO(2) {ECO:0000269|PubMed:9882445};
CC Vmax=2.5 umol/min/mg enzyme with CO(2) as substrate
CC {ECO:0000269|PubMed:9882445};
CC Note=The CO(2)/O(2) specificity factor (tau) is 39.;
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains
CC (PubMed:9882445, PubMed:17574029, PubMed:7922027); disulfide-linked
CC (PubMed:8245022). The disulfide link is formed within the large subunit
CC homodimers (PubMed:8245022, PubMed:7922027, PubMed:17574029)
CC (Probable). The exposed C-terminus binds in a cleft in the RbcX2 (shown
CC with endogenous and Anabaena strain CA protein) (PubMed:20075914,
CC PubMed:21765418). RbcX2 is displaced by RbcS; as RbcX2 is removed RbcS
CC mediates the ordering of an internal RbcL loop (Thr-64-Leu-70) in a
CC catalytically active conformation (PubMed:17574029, PubMed:21765418)
CC (Probable). {ECO:0000269|PubMed:17574029, ECO:0000269|PubMed:20075914,
CC ECO:0000269|PubMed:21765418, ECO:0000269|PubMed:7922027,
CC ECO:0000269|PubMed:8245022, ECO:0000305|PubMed:20075914,
CC ECO:0000305|PubMed:21765418, ECO:0000305|PubMed:9882445}.
CC -!- INTERACTION:
CC P00880; A0A0H3K9R3: rbcX; NbExp=3; IntAct=EBI-9023246, EBI-15936812;
CC P00880; Q44212: rbcX; Xeno; NbExp=3; IntAct=EBI-9023246, EBI-9023244;
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338}.
CC Note=In the carboxysome RuBisCO is organized into a paracrystalline
CC array (By similarity). This cyanobacterium makes beta-type carboxysomes
CC (Probable). {ECO:0000250|UniProtKB:Q31NB3, ECO:0000305}.
CC -!- DOMAIN: Binding of RbcS probably induces a conformation change that
CC displaces RbcX2 and triggers the final mature conformation.
CC {ECO:0000269|PubMed:21765418, ECO:0000305|PubMed:20075914}.
CC -!- PTM: The disulfide bond which can form in the large chain dimeric
CC partners within the hexadecamer appears to be associated with oxidative
CC stress and protein turnover. {ECO:0000305|PubMed:8245022}.
CC -!- MISCELLANEOUS: RuBisCO folding and assembly commences when the nascent
CC large subunit folds with the help of the chaperonin GroEL-GroES.
CC Monomers require chaperone RbcX2 to assemble into RbcL8 octamers
CC yielding RbcL8-(RbcX2)8 (PubMed:17574029) (Probable). RbcX2 is
CC displaced by RbcS; as RbcX2 is removed RbcS mediates the ordering of an
CC internal RbcL loop (Thr-64-Leu-70) in a catalytically active
CC conformation (PubMed:17574029, PubMed:21765418) (Probable).
CC {ECO:0000269|PubMed:17574029, ECO:0000269|PubMed:21765418,
CC ECO:0000305|PubMed:20075914, ECO:0000305|PubMed:21765418}.
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:0000269|PubMed:8245022}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000305}.
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DR EMBL; K00486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X03220; CAA26972.1; -; Genomic_DNA.
DR EMBL; AP008231; BAD78320.1; -; Genomic_DNA.
DR PIR; A90941; RKYCL.
DR RefSeq; WP_011242444.1; NZ_CP085785.1.
DR PDB; 1RBL; X-ray; 2.20 A; A/B/C/D/E/F/G/H=6-472.
DR PDB; 1RSC; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-472.
DR PDB; 2WVW; EM; 9.00 A; A/B/C/D/E/F/G/H=1-472.
DR PDB; 3RG6; X-ray; 3.20 A; A/B=1-472.
DR PDB; 8ILB; EM; 3.00 A; A/B/C/D/J/K/L/M=1-472.
DR PDB; 8ILM; EM; 3.30 A; A/B/F/G/H/I/J/K=1-472.
DR PDB; 8IO2; EM; 3.10 A; A/B/C/D/E/F/G/H=2-472.
DR PDB; 8IOJ; EM; 4.10 A; A/B/C/D/H/I/J/K=1-472.
DR PDB; 8IOL; EM; 2.90 A; A/B/C/D/E/F/G/H=1-472.
DR PDBsum; 1RBL; -.
DR PDBsum; 1RSC; -.
DR PDBsum; 2WVW; -.
DR PDBsum; 3RG6; -.
DR PDBsum; 8ILB; -.
DR PDBsum; 8ILM; -.
DR PDBsum; 8IO2; -.
DR PDBsum; 8IOJ; -.
DR PDBsum; 8IOL; -.
DR AlphaFoldDB; P00880; -.
DR EMDB; EMD-35532; -.
DR EMDB; EMD-35536; -.
DR EMDB; EMD-35605; -.
DR EMDB; EMD-35620; -.
DR EMDB; EMD-35621; -.
DR SMR; P00880; -.
DR DIP; DIP-6210N; -.
DR IntAct; P00880; 2.
DR GeneID; 76400167; -.
DR KEGG; syc:syc0130_c; -.
DR eggNOG; COG1850; Bacteria.
DR SABIO-RK; P00880; -.
DR EvolutionaryTrace; P00880; -.
DR Proteomes; UP000001175; 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:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR CDD; cd08212; RuBisCO_large_I; 1.
DR DisProt; DP02960; -.
DR Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 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; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDG01052; RuBisCO; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 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; Direct protein sequencing;
KW Disulfide bond; Lyase; Magnesium; Metal-binding; Monooxygenase;
KW Oxidoreductase; Photorespiration; Photosynthesis.
FT CHAIN 1..472
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062651"
FT MOTIF 461..467
FT /note="Interacts with RbcX2"
FT /evidence="ECO:0000269|PubMed:17574029"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT ACT_SITE 291
FT /note="Proton acceptor"
FT BINDING 120
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT BINDING 170
FT /ligand="substrate"
FT BINDING 174
FT /ligand="substrate"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000269|PubMed:8245022"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:8245022"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:8245022"
FT BINDING 292
FT /ligand="substrate"
FT BINDING 324
FT /ligand="substrate"
FT BINDING 376
FT /ligand="substrate"
FT SITE 331
FT /note="Transition state stabilizer"
FT MOD_RES 198
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:16593333"
FT DISULFID 244
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000269|PubMed:8245022"
FT MUTAGEN 49
FT /note="E->A,C: Does not form the RbcL8-(RbcX2)8 complex."
FT /evidence="ECO:0000269|PubMed:21765418"
FT MUTAGEN 53
FT /note="A->H: Wild-type formation of the RbcL8-(RbcX2)8
FT complex."
FT /evidence="ECO:0000269|PubMed:21765418"
FT MUTAGEN 67..71
FT /note="WTDLL->ATDGA: Alters the RbcL-RbcS interface, RbcS
FT cannot displace RbcX2 from assembly intermediate."
FT /evidence="ECO:0000269|PubMed:21765418"
FT MUTAGEN 106
FT /note="E->Q: Protein aggregates, forms RbcL2-RbcX(2)2
FT homodimer intermediate poorly."
FT /evidence="ECO:0000269|PubMed:21765418"
FT MUTAGEN 126
FT /note="A->Y: Reduced formation of the RbcL8-(RbcX2)8
FT complex."
FT /evidence="ECO:0000269|PubMed:21765418"
FT MUTAGEN 212
FT /note="R->S: Forms stable homodimer in presence of RbcX2
FT but does not form RbcL8 form."
FT /evidence="ECO:0000269|PubMed:21765418"
FT MUTAGEN 461..472
FT /note="Missing: Remains bound to GroEL."
FT /evidence="ECO:0000269|PubMed:20075914"
FT MUTAGEN 464
FT /note="F->A: Remains bound to GroEL."
FT /evidence="ECO:0000269|PubMed:20075914"
FT MUTAGEN 466
FT /note="F->A: Remains bound to GroEL."
FT /evidence="ECO:0000269|PubMed:20075914"
FT CONFLICT 38..39
FT /note="RF -> PV (in Ref. 1; K00486)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="A -> R (in Ref. 1; K00486)"
FT /evidence="ECO:0000305"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:1RBL"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 211..229
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 336..347
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 384..391
FT /evidence="ECO:0007829|PDB:1RBL"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 410..430
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 434..448
FT /evidence="ECO:0007829|PDB:1RBL"
FT HELIX 450..459
FT /evidence="ECO:0007829|PDB:1RBL"
SQ SEQUENCE 472 AA; 52448 MW; CDD8519AA9D493C9 CRC64;
MPKTQSAAGY KAGVKDYKLT YYTPDYTPKD TDLLAAFRFS PQPGVPADEA GAAIAAESST
GTWTTVWTDL LTDMDRYKGK CYHIEPVQGE ENSYFAFIAY PLDLFEEGSV TNILTSIVGN
VFGFKAIRSL RLEDIRFPVA LVKTFQGPPH GIQVERDLLN KYGRPMLGCT IKPKLGLSAK
NYGRAVYECL RGGLDFTKDD ENINSQPFQR WRDRFLFVAD AIHKSQAETG EIKGHYLNVT
APTCEEMMKR AEFAKELGMP IIMHDFLTAG FTANTTLAKW CRDNGVLLHI HRAMHAVIDR
QRNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGDKASTL GFVDLMREDH IEADRSRGVF
FTQDWASMPG VLPVASGGIH VWHMPALVEI FGDDSVLQFG GGTLGHPWGN APGATANRVA
LEACVQARNE GRDLYREGGD ILREAGKWSP ELAAALDLWK EIKFEFETMD KL
//
