CABC1_PROVU
ID CABC1_PROVU Reviewed; 1021 AA.
AC P59807; D0V0C9;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Chondroitin sulfate ABC endolyase;
DE EC=4.2.2.20;
DE AltName: Full=Chondroitin ABC endoeliminase;
DE AltName: Full=Chondroitin ABC lyase I;
DE AltName: Full=Chondroitin sulfate ABC lyase I;
DE Short=ChS ABC lyase I;
DE AltName: Full=Chondroitinase ABC I;
DE Short=cABC I;
DE AltName: Full=Endochondroitinase ABC;
DE AltName: INN=Condoliase;
DE Flags: Precursor;
OS Proteus vulgaris.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=585;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-42, CATALYTIC
RP ACTIVITY, AND INDUCTION.
RC STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
RX PubMed=7512814; DOI=10.1007/bf00166079;
RA Sato N., Shimada M., Nakajima H., Oda H., Kimura S.;
RT "Cloning and expression in Escherichia coli of the gene encoding the
RT Proteus vulgaris chondroitin ABC lyase.";
RL Appl. Microbiol. Biotechnol. 41:39-46(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ryan M.J., Khandke K.M., Tilley B.C., Lotvin J.A.;
RT "Cloning and expression of the chondroitinase I and II genes from Proteus
RT vulgaris.";
RL Patent number WO9425567, 10-NOV-1994.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-1021.
RC STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
RA Tam K.W., Wang Q., Li R.A., Chan Y.S., Shum D.K.Y.;
RT "Use of chondroitin sulfate lyases in combination for promotion of neurite
RT growth.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
RX PubMed=9083041; DOI=10.1074/jbc.272.14.9123;
RA Hamai A., Hashimoto N., Mochizuki H., Kato F., Makiguchi Y., Horie K.,
RA Suzuki S.;
RT "Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding
RT tetrasaccharides and an exoeliminase preferentially acting on
RT oligosaccharides.";
RL J. Biol. Chem. 272:9123-9130(1997).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVE SITE RESIDUES, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-500; HIS-501; TYR-508; ARG-560; HIS-561; GLU-653 AND HIS-712.
RC STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
RX PubMed=15691229; DOI=10.1042/bj20041222;
RA Prabhakar V., Capila I., Bosques C.J., Pojasek K., Sasisekharan R.;
RT "Chondroitinase ABC I from Proteus vulgaris: cloning, recombinant
RT expression and active site identification.";
RL Biochem. J. 386:103-112(2005).
RN [6]
RP CATALYTIC ACTIVITY, ACTIVE SITE RESIDUES, AND MUTAGENESIS OF ARG-500;
RP HIS-501; TYR-508; ARG-560 AND GLU-653.
RC STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
RX PubMed=16108757; DOI=10.1042/bj20050532;
RA Prabhakar V., Raman R., Capila I., Bosques C.J., Pojasek K.,
RA Sasisekharan R.;
RT "Biochemical characterization of the chondroitinase ABC I active site.";
RL Biochem. J. 390:395-405(2005).
RN [7]
RP ROLE IN DAMAGED CNS RECOVERY.
RX PubMed=17572406; DOI=10.1016/j.expneurol.2007.05.001;
RA Crespo D., Asher R.A., Lin R., Rhodes K.E., Fawcett J.W.;
RT "How does chondroitinase promote functional recovery in the damaged CNS?";
RL Exp. Neurol. 206:159-171(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SODIUM ION, DOMAIN,
RP AND DISCUSSION OF SEQUENCE.
RC STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
RX PubMed=12706721; DOI=10.1016/s0022-2836(03)00345-0;
RA Huang W., Lunin V.V., Li Y., Suzuki S., Sugiura N., Miyazono H., Cygler M.;
RT "Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at
RT 1.9A resolution.";
RL J. Mol. Biol. 328:623-634(2003).
CC -!- FUNCTION: Endolytic, broad-specificity glycosaminoglycan lyase, which
CC degrades the polysaccharides chondroitin, chondroitin-4-sulfate,
CC chondroitin-6-sulfate, dermatan sulfate and to a lesser extent
CC hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to
CC unsaturated tetrasaccharides and disaccharides. Is not active against
CC keratan sulfate, heparan sulfate, and heparin. Is able to promote
CC functional recovery in the injured central nervous system (CNS), via
CC its role in the disruption of the normal organization of the
CC extracellular matrix (ECM). {ECO:0000269|PubMed:15691229,
CC ECO:0000269|PubMed:17572406, ECO:0000269|PubMed:9083041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endolytic cleavage of (1->4)-beta-galactosaminic bonds between
CC N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid
CC to produce a mixture of Delta(4)-unsaturated oligosaccharides of
CC different sizes that are ultimately degraded to Delta(4)-unsaturated
CC tetra- and disaccharides.; EC=4.2.2.20;
CC Evidence={ECO:0000269|PubMed:15691229, ECO:0000269|PubMed:16108757,
CC ECO:0000269|PubMed:7512814, ECO:0000269|PubMed:9083041};
CC -!- ACTIVITY REGULATION: Is inhibited by Zn(2+), Ni(2+), Fe(2+) and Cu(2+).
CC {ECO:0000269|PubMed:9083041}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=66 uM for chondroitin 6-sulfate {ECO:0000269|PubMed:15691229,
CC ECO:0000269|PubMed:9083041};
CC KM=1.2 uM for chondroitin 6-sulfate {ECO:0000269|PubMed:15691229,
CC ECO:0000269|PubMed:9083041};
CC KM=1.5 uM for chondroitin 4-sulfate {ECO:0000269|PubMed:15691229,
CC ECO:0000269|PubMed:9083041};
CC KM=2.5 uM for dermatan sulfate {ECO:0000269|PubMed:15691229,
CC ECO:0000269|PubMed:9083041};
CC Vmax=310 umol/min/mg enzyme with chondroitin 6-sulfate as substrate
CC {ECO:0000269|PubMed:15691229, ECO:0000269|PubMed:9083041};
CC pH dependence:
CC Optimum pH is 8. Is essentially inactive at pH 9.0.
CC {ECO:0000269|PubMed:15691229, ECO:0000269|PubMed:9083041};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:15691229, ECO:0000269|PubMed:9083041};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12706721}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:15691229}.
CC -!- INDUCTION: By chondroitin sulfate or its degraded products.
CC {ECO:0000269|PubMed:7512814}.
CC -!- DOMAIN: Consists of three domains. The middle domain contains the
CC catalytic site in a wide-open cleft. {ECO:0000269|PubMed:12706721}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:7512814 shows amino acid differences at positions 317,
CC 321, 410, 694, 738 and 866 due to incorrect translation of the
CC nucleotide sequence. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; GQ996964; ACY01450.1; -; Genomic_DNA.
DR PDB; 1HN0; X-ray; 1.90 A; A=1-1021.
DR PDB; 7EIP; X-ray; 1.88 A; A=1-1021.
DR PDB; 7EIQ; X-ray; 1.80 A; A=1-1021.
DR PDB; 7EIR; X-ray; 1.92 A; A=1-1021.
DR PDB; 7EIS; X-ray; 2.50 A; A=1-1021.
DR PDBsum; 1HN0; -.
DR PDBsum; 7EIP; -.
DR PDBsum; 7EIQ; -.
DR PDBsum; 7EIR; -.
DR PDBsum; 7EIS; -.
DR AlphaFoldDB; P59807; -.
DR SMR; P59807; -.
DR IntAct; P59807; 2.
DR MINT; P59807; -.
DR STRING; 585.DR95_2846; -.
DR CAZy; PL8; Polysaccharide Lyase Family 8.
DR eggNOG; ENOG502Z8J1; Bacteria.
DR BioCyc; MetaCyc:MON-15788; -.
DR BRENDA; 4.2.2.20; 5049.
DR EvolutionaryTrace; P59807; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0034000; F:chondroitin-sulfate-ABC endolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.100; -; 1.
DR Gene3D; 2.60.220.10; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR039174; Chondroitin_ABC_lyase.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR024200; Chondroitinase_ABC_I.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR011071; Lyase_8-like_C.
DR InterPro; IPR003159; Lyase_8_central_dom.
DR InterPro; IPR015177; Lyase_catalyt.
DR InterPro; IPR015176; Lyase_N.
DR PANTHER; PTHR37322; PTHR37322; 1.
DR Pfam; PF02278; Lyase_8; 1.
DR Pfam; PF09093; Lyase_catalyt; 1.
DR Pfam; PF09092; Lyase_N; 1.
DR PIRSF; PIRSF034515; Chondroitinase; 1.
DR SUPFAM; SSF48230; SSF48230; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49863; SSF49863; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW Lyase; Metal-binding; Periplasm; Signal; Sodium.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:7512814"
FT CHAIN 25..1021
FT /note="Chondroitin sulfate ABC endolyase"
FT /id="PRO_0000024929"
FT ACT_SITE 501
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:15691229,
FT ECO:0000269|PubMed:16108757"
FT ACT_SITE 508
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 43
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:12706721,
FT ECO:0007744|PDB:1HN0"
FT BINDING 70
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:12706721,
FT ECO:0007744|PDB:1HN0"
FT BINDING 73
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:12706721,
FT ECO:0007744|PDB:1HN0"
FT BINDING 211
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:12706721,
FT ECO:0007744|PDB:1HN0"
FT SITE 560
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT SITE 653
FT /note="Important for catalytic activity"
FT MUTAGEN 500
FT /note="R->A: Still active on both chondroitin 6-sulfate and
FT dermatan sulfate, but with highly reduced catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:15691229,
FT ECO:0000269|PubMed:16108757"
FT MUTAGEN 501
FT /note="H->A,K,R: Loss of activity on both chondroitin 6-
FT sulfate and dermatan sulfate."
FT /evidence="ECO:0000269|PubMed:15691229,
FT ECO:0000269|PubMed:16108757"
FT MUTAGEN 508
FT /note="Y->A: Loss of activity on both chondroitin 6-sulfate
FT and dermatan sulfate."
FT /evidence="ECO:0000269|PubMed:15691229,
FT ECO:0000269|PubMed:16108757"
FT MUTAGEN 508
FT /note="Y->F: Still active on both chondroitin 6-sulfate and
FT dermatan sulfate, but with greatly reduced catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:15691229,
FT ECO:0000269|PubMed:16108757"
FT MUTAGEN 560
FT /note="R->A: Loss of activity on both chondroitin 6-sulfate
FT and dermatan sulfate."
FT /evidence="ECO:0000269|PubMed:15691229,
FT ECO:0000269|PubMed:16108757"
FT MUTAGEN 561
FT /note="H->A: Still active on both chondroitin 6-sulfate and
FT dermatan sulfate, but with reduced catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:15691229"
FT MUTAGEN 653
FT /note="E->A,D: Loss of activity on both chondroitin 6-
FT sulfate and dermatan sulfate."
FT /evidence="ECO:0000269|PubMed:15691229,
FT ECO:0000269|PubMed:16108757"
FT MUTAGEN 653
FT /note="E->Q: Still active on both chondroitin 6-sulfate and
FT dermatan sulfate, but with reduced catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:15691229,
FT ECO:0000269|PubMed:16108757"
FT MUTAGEN 712
FT /note="H->A: Still active on both chondroitin 6-sulfate and
FT dermatan sulfate, but with reduced catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:15691229"
FT CONFLICT 125
FT /note="L -> P (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="M -> V (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="A -> G (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="S -> R (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 104..119
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:7EIQ"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 203..219
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 251..269
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:7EIR"
FT HELIX 313..317
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 324..330
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 336..352
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 356..375
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 390..403
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 414..424
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:7EIQ"
FT TURN 438..441
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 443..448
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 450..458
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 463..482
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 506..523
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 532..547
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 549..553
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 572..580
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 588..598
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 602..609
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 630..635
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 638..643
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:1HN0"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 667..676
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 679..681
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 703..706
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 709..712
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 719..721
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 724..728
FT /evidence="ECO:0007829|PDB:7EIQ"
FT TURN 729..731
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 732..740
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 753..761
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 764..773
FT /evidence="ECO:0007829|PDB:7EIQ"
FT TURN 775..780
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 781..789
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:7EIP"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 802..804
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 807..813
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 818..820
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 826..831
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 835..845
FT /evidence="ECO:0007829|PDB:7EIQ"
FT TURN 847..849
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 852..863
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 864..866
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 867..878
FT /evidence="ECO:0007829|PDB:7EIQ"
FT HELIX 883..894
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 898..914
FT /evidence="ECO:0007829|PDB:7EIQ"
FT TURN 915..918
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 919..926
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 933..949
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 952..958
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 966..968
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 973..981
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 983..986
FT /evidence="ECO:0007829|PDB:1HN0"
FT STRAND 993..997
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 1000..1008
FT /evidence="ECO:0007829|PDB:7EIQ"
FT STRAND 1013..1019
FT /evidence="ECO:0007829|PDB:7EIQ"
SQ SEQUENCE 1021 AA; 115092 MW; 299406E6466568AC CRC64;
MPIFRFTALA MTLGLLSAPY NAMAATSNPA FDPKNLMQSE IYHFAQNNPL ADFSSDKNSI
LTLSDKRSIM GNQSLLWKWK GGSSFTLHKK LIVPTDKEAS KAWGRSSTPV FSFWLYNEKP
IDGYLTIDFG EKLISTSEAQ AGFKVKLDFT GWRAVGVSLN NDLENREMTL NATNTSSDGT
QDSIGRSLGA KVDSIRFKAP SNVSQGEIYI DRIMFSVDDA RYQWSDYQVK TRLSEPEIQF
HNVKPQLPVT PENLAAIDLI RQRLINEFVG GEKETNLALE ENISKLKSDF DALNIHTLAN
GGTQGRHLIT DKQIIIYQPE NLNSQDKQLF DNYVILGNYT TLMFNISRAY VLEKDPTQKA
QLKQMYLLMT KHLLDQGFVK GSALVTTHHW GYSSRWWYIS TLLMSDALKE ANLQTQVYDS
LLWYSREFKS SFDMKVSADS SDLDYFNTLS RQHLALLLLE PDDQKRINLV NTFSHYITGA
LTQVPPGGKD GLRPDGTAWR HEGNYPGYSF PAFKNASQLI YLLRDTPFSV GESGWNNLKK
AMVSAWIYSN PEVGLPLAGR HPFNSPSLKS VAQGYYWLAM SAKSSPDKTL ASIYLAISDK
TQNESTAIFG ETITPASLPQ GFYAFNGGAF GIHRWQDKMV TLKAYNTNVW SSEIYNKDNR
YGRYQSHGVA QIVSNGSQLS QGYQQEGWDW NRMQGATTIH LPLKDLDSPK PHTLMQRGER
GFSGTSSLEG QYGMMAFDLI YPANLERFDP NFTAKKSVLA ADNHLIFIGS NINSSDKNKN
VETTLFQHAI TPTLNTLWIN GQKIENMPYQ TTLQQGDWLI DSNGNGYLIT QAEKVNVSRQ
HQVSAENKNR QPTEGNFSSA WIDHSTRPKD ASYEYMVFLD ATPEKMGEMA QKFRENNGLY
QVLRKDKDVH IILDKLSNVT GYAFYQPASI EDKWIKKVNK PAIVMTHRQK DTLIVSAVTP
DLNMTRQKAA TPVTINVTIN GKWQSADKNS EVKYQVSGDN TELTFTSYFG IPQEIKLSPL
P
