NADE_MYCTU
ID NADE_MYCTU Reviewed; 679 AA.
AC P9WJJ3; L0T9M3; P0A5L6; P71911;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_02090, ECO:0000303|PubMed:19270703, ECO:0000303|PubMed:22280445};
DE EC=6.3.5.1 {ECO:0000255|HAMAP-Rule:MF_02090, ECO:0000269|PubMed:15748981, ECO:0000269|PubMed:19270703, ECO:0000269|PubMed:9620974};
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_02090};
GN Name=nadE {ECO:0000255|HAMAP-Rule:MF_02090}; OrderedLocusNames=Rv2438c;
GN ORFNames=MTCY428.08;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9620974; DOI=10.1128/jb.180.12.3218-3221.1998;
RA Cantoni R., Branzoni M., Labo M., Rizzi M., Riccardi G.;
RT "The MTCY428.08 gene of Mycobacterium tuberculosis codes for NAD+
RT synthetase.";
RL J. Bacteriol. 180:3218-3221(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-52; LYS-121 AND CYS-176,
RP AND ACTIVE SITE.
RX PubMed=15748981; DOI=10.1016/j.resmic.2004.08.011;
RA Bellinzoni M., Buroni S., Pasca M.R., Guglierame P., Arcesi F.,
RA De Rossi E., Riccardi G.;
RT "Glutamine amidotransferase activity of NAD+ synthetase from Mycobacterium
RT tuberculosis depends on an amino-terminal nitrilase domain.";
RL Res. Microbiol. 156:173-177(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5] {ECO:0007744|PDB:3DLA}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH DEAMIDO-NAD,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, DOMAIN, ACTIVE SITE, AND MUTAGENESIS OF ASP-656.
RX PubMed=19270703; DOI=10.1038/nsmb.1567;
RA LaRonde-LeBlanc N., Resto M., Gerratana B.;
RT "Regulation of active site coupling in glutamine-dependent NAD(+)
RT synthetase.";
RL Nat. Struct. Mol. Biol. 16:421-429(2009).
RN [6] {ECO:0007744|PDB:3SDB, ECO:0007744|PDB:3SEQ, ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SYT, ECO:0007744|PDB:3SZG}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH AMP; ATP; L-GLUTAMIC
RP ACID; NAD; DEAMIDO-NAD AND DIPHOSPHATE, ACTIVITY REGULATION, SUBUNIT, AND
RP DOMAIN.
RX PubMed=22280445; DOI=10.1042/bj20112210;
RA Chuenchor W., Doukov T.I., Resto M., Chang A., Gerratana B.;
RT "Regulation of the intersubunit ammonia tunnel in Mycobacterium
RT tuberculosis glutamine-dependent NAD+ synthetase.";
RL Biochem. J. 443:417-426(2012).
CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC NAD. Uses L-glutamine as a nitrogen source. In vitro, can also use
CC ammonia with comparable specific activity.
CC {ECO:0000269|PubMed:15748981, ECO:0000269|PubMed:19270703,
CC ECO:0000269|PubMed:9620974}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate +
CC H(+) + L-glutamate + NAD(+); Xref=Rhea:RHEA:24384, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.5.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02090,
CC ECO:0000269|PubMed:15748981, ECO:0000269|PubMed:19270703,
CC ECO:0000269|PubMed:9620974};
CC -!- ACTIVITY REGULATION: The formation of the intermediates complex at the
CC synthetase domain stimulates the glutaminase activity.
CC {ECO:0000269|PubMed:22280445}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for glutamine {ECO:0000269|PubMed:19270703};
CC KM=0.13 mM for deamido-NAD(+) (with glutamine as a nitrogen source)
CC {ECO:0000269|PubMed:19270703};
CC KM=0.12 mM for ATP (with glutamine as a nitrogen source)
CC {ECO:0000269|PubMed:19270703};
CC KM=20 mM for ammonia {ECO:0000269|PubMed:19270703};
CC KM=0.7 mM for deamido-NAD(+) (with ammonia as a nitrogen source)
CC {ECO:0000269|PubMed:19270703};
CC KM=1.4 mM for ATP (with ammonia as a nitrogen source)
CC {ECO:0000269|PubMed:19270703};
CC Note=kcat is 0.55 sec(-1) for glutamine-dependent activity. kcat is
CC 2.8 sec(-1) for ammonia-dependent activity.
CC {ECO:0000269|PubMed:19270703};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_02090, ECO:0000305|PubMed:19270703}.
CC -!- SUBUNIT: Homooctamer; composed of two stacked homotetramers that form a
CC ring-like structure. {ECO:0000269|PubMed:19270703,
CC ECO:0000269|PubMed:22280445}.
CC -!- INTERACTION:
CC P9WJJ3; P9WJJ3: nadE; NbExp=2; IntAct=EBI-15763158, EBI-15763158;
CC -!- DOMAIN: An ammonia tunnel 40 Angstroms long allows transfer of ammonia
CC from the glutaminase active site, where it is produced, to the
CC synthetase active site, where it is used for the ATP-dependent
CC formation of NAD(+). {ECO:0000269|PubMed:19270703,
CC ECO:0000269|PubMed:22280445}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {ECO:0000255|HAMAP-Rule:MF_02090, ECO:0000305}.
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DR EMBL; AL123456; CCP45230.1; -; Genomic_DNA.
DR PIR; D70680; D70680.
DR RefSeq; NP_216954.2; NC_000962.3.
DR RefSeq; WP_003901403.1; NZ_NVQJ01000024.1.
DR PDB; 3DLA; X-ray; 2.35 A; A/B/C/D=1-679.
DR PDB; 3SDB; X-ray; 2.00 A; A=1-679.
DR PDB; 3SEQ; X-ray; 2.73 A; A/B/C/D=1-679.
DR PDB; 3SEZ; X-ray; 2.65 A; A/B/C/D=1-679.
DR PDB; 3SYT; X-ray; 2.65 A; A/B/C/D=1-679.
DR PDB; 3SZG; X-ray; 2.25 A; A/B/C/D=1-679.
DR PDBsum; 3DLA; -.
DR PDBsum; 3SDB; -.
DR PDBsum; 3SEQ; -.
DR PDBsum; 3SEZ; -.
DR PDBsum; 3SYT; -.
DR PDBsum; 3SZG; -.
DR AlphaFoldDB; P9WJJ3; -.
DR SMR; P9WJJ3; -.
DR STRING; 83332.Rv2438c; -.
DR PaxDb; P9WJJ3; -.
DR DNASU; 885808; -.
DR GeneID; 45426428; -.
DR GeneID; 885808; -.
DR KEGG; mtu:Rv2438c; -.
DR TubercuList; Rv2438c; -.
DR eggNOG; COG0171; Bacteria.
DR eggNOG; COG0388; Bacteria.
DR OMA; RLAQDCY; -.
DR PhylomeDB; P9WJJ3; -.
DR BRENDA; 6.3.5.1; 3445.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IDA:MTBBASE.
DR GO; GO:0008795; F:NAD+ synthase activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IDA:MTBBASE.
DR CDD; cd00553; NAD_synthase; 1.
DR Gene3D; 1.10.10.1140; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR HAMAP; MF_02090; NadE_glutamine_dep; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR014445; Gln-dep_NAD_synthase.
DR InterPro; IPR041856; NAD+_synth_C.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR003694; NAD_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR23090; PTHR23090; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PIRSF; PIRSF006630; NADS_GAT; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; NAD; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..679
FT /note="Glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000152241"
FT DOMAIN 12..276
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 337..679
FT /note="Ligase"
FT REGION 639..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 52
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0000305|PubMed:15748981, ECO:0000305|PubMed:19270703"
FT ACT_SITE 121
FT /note="For glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0000305|PubMed:15748981, ECO:0000305|PubMed:19270703"
FT ACT_SITE 176
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0000305|PubMed:15748981, ECO:0000305|PubMed:19270703"
FT BINDING 127
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0007744|PDB:3SYT"
FT BINDING 203
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0007744|PDB:3SYT"
FT BINDING 209
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0007744|PDB:3SYT"
FT BINDING 354
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SEQ,
FT ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SYT,
FT ECO:0007744|PDB:3SZG"
FT BINDING 366..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0007744|PDB:3SEQ, ECO:0007744|PDB:3SEZ,
FT ECO:0007744|PDB:3SYT, ECO:0007744|PDB:3SZG"
FT BINDING 456
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SEQ,
FT ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SZG"
FT BINDING 471
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SEQ,
FT ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SYT,
FT ECO:0007744|PDB:3SZG"
FT BINDING 475
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SEQ,
FT ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SYT,
FT ECO:0007744|PDB:3SZG"
FT BINDING 480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0007744|PDB:3SEQ, ECO:0007744|PDB:3SYT,
FT ECO:0007744|PDB:3SZG"
FT BINDING 485
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0007744|PDB:3SEQ, ECO:0007744|PDB:3SEZ,
FT ECO:0007744|PDB:3SYT"
FT BINDING 490..493
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SEQ,
FT ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SYT,
FT ECO:0007744|PDB:3SZG"
FT BINDING 501
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SEQ,
FT ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SYT,
FT ECO:0007744|PDB:3SZG"
FT BINDING 635
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02090,
FT ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SEQ,
FT ECO:0007744|PDB:3SEZ, ECO:0007744|PDB:3SYT,
FT ECO:0007744|PDB:3SZG"
FT BINDING 661
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0007744|PDB:3DLA, ECO:0007744|PDB:3SZG"
FT MUTAGEN 52
FT /note="E->A: Lack of glutamine-dependent activity. Retains
FT 30% of ammonia-dependent activity."
FT /evidence="ECO:0000269|PubMed:15748981"
FT MUTAGEN 121
FT /note="K->A: Lack of glutamine-dependent and ammonia-
FT dependent activities."
FT /evidence="ECO:0000269|PubMed:15748981"
FT MUTAGEN 176
FT /note="C->A: Lack of glutamine-dependent activity. Retains
FT 90% of ammonia-dependent activity."
FT /evidence="ECO:0000269|PubMed:15748981"
FT MUTAGEN 656
FT /note="D->A: Causes a decrease in ammonia channel
FT efficiency to 70% compared with wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:19270703"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 11..18
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 26..42
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:3SDB"
FT TURN 52..56
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 67..84
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 88..99
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 102..111
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 333..357
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 371..386
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 411..419
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 429..438
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:3SZG"
FT HELIX 453..473
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 483..488
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:3SDB"
FT TURN 504..507
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 510..523
FT /evidence="ECO:0007829|PDB:3SDB"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:3SEQ"
FT HELIX 528..542
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 558..561
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 564..577
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 581..592
FT /evidence="ECO:0007829|PDB:3SDB"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:3SYT"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 614..629
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 633..636
FT /evidence="ECO:0007829|PDB:3SDB"
FT TURN 653..656
FT /evidence="ECO:0007829|PDB:3SDB"
FT HELIX 666..675
FT /evidence="ECO:0007829|PDB:3SDB"
SQ SEQUENCE 679 AA; 74683 MW; 14AC29CE434A8B0D CRC64;
MNFYSAYQHG FVRVAACTHH TTIGDPAANA ASVLDMARAC HDDGAALAVF PELTLSGYSI
EDVLLQDSLL DAVEDALLDL VTESADLLPV LVVGAPLRHR HRIYNTAVVI HRGAVLGVVP
KSYLPTYREF YERRQMAPGD GERGTIRIGG ADVAFGTDLL FAASDLPGFV LHVEICEDMF
VPMPPSAEAA LAGATVLANL SGSPITIGRA EDRRLLARSA SARCLAAYVY AAAGEGESTT
DLAWDGQTMI WENGALLAES ERFPKGVRRS VADVDTELLR SERLRMGTFD DNRRHHRELT
ESFRRIDFAL DPPAGDIGLL REVERFPFVP ADPQRLQQDC YEAYNIQVSG LEQRLRALDY
PKVVIGVSGG LDSTHALIVA THAMDREGRP RSDILAFALP GFATGEHTKN NAIKLARALG
VTFSEIDIGD TARLMLHTIG HPYSVGEKVY DVTFENVQAG LRTDYLFRIA NQRGGIVLGT
GDLSELALGW STYGVGDQMS HYNVNAGVPK TLIQHLIRWV ISAGEFGEKV GEVLQSVLDT
EITPELIPTG EEELQSSEAK VGPFALQDFS LFQVLRYGFR PSKIAFLAWH AWNDAERGNW
PPGFPKSERP SYSLAEIRHW LQIFVQRFYS FSQFKRSALP NGPKVSHGGA LSPRGDWRAP
SDMSARIWLD QIDREVPKG
