PYC_STAAM
ID PYC_STAAM Reviewed; 1150 AA.
AC A0A0H3JRU9;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Pyruvate carboxylase;
DE EC=6.4.1.1 {ECO:0000269|PubMed:19523900, ECO:0000269|PubMed:23286247};
GN Name=pycA; OrderedLocusNames=SAV1114;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2] {ECO:0007744|PDB:3BG5}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP AND PYRUVATE,
RP SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=18297087; DOI=10.1038/nsmb.1393;
RA Xiang S., Tong L.;
RT "Crystal structures of human and Staphylococcus aureus pyruvate carboxylase
RT and molecular insights into the carboxyltransfer reaction.";
RL Nat. Struct. Mol. Biol. 15:295-302(2008).
RN [3] {ECO:0007744|PDB:3HB9, ECO:0007744|PDB:3HBL, ECO:0007744|PDB:3HO8}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) IN COMPLEX WITH MANGANESE, SUBUNIT,
RP MUTAGENESIS OF ALA-580; ARG-614; TYR-621; GLN-838; THR-876; SER-879 AND
RP LYS-880, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=19523900; DOI=10.1016/j.str.2009.04.008;
RA Yu L.P., Xiang S., Lasso G., Gil D., Valle M., Tong L.;
RT "A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with
RT coenzyme A.";
RL Structure 17:823-832(2009).
RN [4] {ECO:0007744|PDB:4HNT, ECO:0007744|PDB:4HNU, ECO:0007744|PDB:4HNV}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP AND MANGANESE,
RP MUTAGENESIS OF ARG-21 AND LYS-411, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY,
RP AND COFACTOR.
RX PubMed=23286247; DOI=10.1021/bi301294d;
RA Yu L.P., Chou C.Y., Choi P.H., Tong L.;
RT "Characterizing the importance of the biotin carboxylase domain dimer for
RT Staphylococcus aureus pyruvate carboxylase catalysis.";
RL Biochemistry 52:488-496(2013).
CC -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC carboxylation of the covalently attached biotin in the first step and
CC the transfer of the carboxyl group to pyruvate in the second.
CC {ECO:0000269|PubMed:19523900, ECO:0000269|PubMed:23286247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1;
CC Evidence={ECO:0000269|PubMed:19523900, ECO:0000269|PubMed:23286247};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000269|PubMed:19523900, ECO:0000269|PubMed:23286247};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18297087,
CC ECO:0000269|PubMed:19523900, ECO:0000269|PubMed:23286247}.
CC -!- INTERACTION:
CC A0A0H3JRU9; A0A0H3JRU9: pycA; NbExp=9; IntAct=EBI-16108775, EBI-16108775;
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; BA000017; BAB57276.1; -; Genomic_DNA.
DR RefSeq; WP_000809514.1; NC_002758.2.
DR PDB; 3BG5; X-ray; 2.80 A; A/B/C/D=1-1150.
DR PDB; 3HB9; X-ray; 2.90 A; A/B/C/D=1-1150.
DR PDB; 3HBL; X-ray; 2.71 A; A/B/C/D=1-1150.
DR PDB; 3HO8; X-ray; 2.90 A; A/B/C/D=1-1150.
DR PDB; 4HNT; X-ray; 2.80 A; A/B/C/D=1-1150.
DR PDB; 4HNU; X-ray; 3.00 A; A/B/C/D=1-1150.
DR PDB; 4HNV; X-ray; 2.80 A; A/B/C/D=1-1150.
DR PDBsum; 3BG5; -.
DR PDBsum; 3HB9; -.
DR PDBsum; 3HBL; -.
DR PDBsum; 3HO8; -.
DR PDBsum; 4HNT; -.
DR PDBsum; 4HNU; -.
DR PDBsum; 4HNV; -.
DR AlphaFoldDB; A0A0H3JRU9; -.
DR SMR; A0A0H3JRU9; -.
DR DrugBank; DB07497; 5-(hexahydro-2-oxo-1H-thieno[3,4-D]imidazol-6-yl)pentanal.
DR PaxDb; A0A0H3JRU9; -.
DR EnsemblBacteria; BAB57276; BAB57276; SAV1114.
DR KEGG; sav:SAV1114; -.
DR HOGENOM; CLU_000395_0_1_9; -.
DR OMA; YAIQSRV; -.
DR PhylomeDB; A0A0H3JRU9; -.
DR BioCyc; SAUR158878:SAV_RS06000-MON; -.
DR BRENDA; 6.4.1.1; 3352.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR005930; Pyruv_COase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01235; pyruv_carbox; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biotin; Ligase; Manganese; Metal-binding;
KW Nucleotide-binding; Pyruvate.
FT CHAIN 1..1150
FT /note="Pyruvate carboxylase"
FT /id="PRO_0000447880"
FT DOMAIN 3..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT DOMAIN 123..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 533..802
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT DOMAIN 1071..1146
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT ACT_SITE 294
FT /evidence="ECO:0000250|UniProtKB:Q9KWU4"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19523900,
FT ECO:0000269|PubMed:23286247, ECO:0007744|PDB:3BG5,
FT ECO:0007744|PDB:4HNT"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19523900,
FT ECO:0007744|PDB:3BG5"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19523900,
FT ECO:0000269|PubMed:23286247, ECO:0007744|PDB:3BG5,
FT ECO:0007744|PDB:4HNT, ECO:0007744|PDB:4HNV"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19523900,
FT ECO:0000269|PubMed:23286247, ECO:0007744|PDB:3BG5,
FT ECO:0007744|PDB:4HNT, ECO:0007744|PDB:4HNV"
FT BINDING 541..545
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19523900,
FT ECO:0007744|PDB:3BG5"
FT BINDING 542
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19523900,
FT ECO:0000269|PubMed:23286247, ECO:0007744|PDB:3HB9,
FT ECO:0007744|PDB:3HBL, ECO:0007744|PDB:4HNT"
FT BINDING 712
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19523900,
FT ECO:0000269|PubMed:23286247, ECO:0007744|PDB:3HB9,
FT ECO:0007744|PDB:3HBL, ECO:0007744|PDB:4HNV"
FT BINDING 741
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19523900,
FT ECO:0000269|PubMed:23286247, ECO:0007744|PDB:3HB9,
FT ECO:0007744|PDB:3HBL, ECO:0007744|PDB:4HNT"
FT BINDING 743
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19523900,
FT ECO:0000269|PubMed:23286247, ECO:0007744|PDB:3HB9,
FT ECO:0007744|PDB:3HBL, ECO:0007744|PDB:4HNT"
FT MOD_RES 712
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:P11498"
FT MOD_RES 1112
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MUTAGEN 21
FT /note="R->A: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:23286247"
FT MUTAGEN 411
FT /note="K->A: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:23286247"
FT MUTAGEN 580
FT /note="A->T: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:19523900"
FT MUTAGEN 614
FT /note="R->A: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:19523900"
FT MUTAGEN 621
FT /note="Y->A: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:19523900"
FT MUTAGEN 838
FT /note="Q->A: About 2.5-fold loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:19523900"
FT MUTAGEN 876
FT /note="T->A: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:19523900"
FT MUTAGEN 879
FT /note="S->A: About 2-fold loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:19523900"
FT MUTAGEN 880
FT /note="K->T: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:19523900"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4HNV"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3HBL"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:3HBL"
FT TURN 146..150
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:4HNT"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 224..238
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:4HNT"
FT HELIX 252..268
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 273..282
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:3HBL"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 374..380
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:4HNT"
FT STRAND 395..404
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 405..418
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 428..436
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 438..442
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 465..479
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 502..506
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 511..527
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 531..537
FT /evidence="ECO:0007829|PDB:3HBL"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 542..547
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 554..567
FT /evidence="ECO:0007829|PDB:3HBL"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 572..578
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 581..587
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 593..603
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 606..614
FT /evidence="ECO:0007829|PDB:3HBL"
FT TURN 615..617
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 620..622
FT /evidence="ECO:0007829|PDB:4HNV"
FT HELIX 626..638
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 643..647
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 653..656
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 657..665
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 669..675
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 680..682
FT /evidence="ECO:0007829|PDB:3HO8"
FT TURN 683..685
FT /evidence="ECO:0007829|PDB:3BG5"
FT STRAND 687..690
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 691..703
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 707..713
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 720..733
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 738..742
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 744..747
FT /evidence="ECO:0007829|PDB:3HB9"
FT HELIX 749..758
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 762..767
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 769..771
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 780..786
FT /evidence="ECO:0007829|PDB:3HBL"
FT TURN 787..789
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:3HO8"
FT HELIX 798..812
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 813..818
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 829..832
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 838..848
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 852..854
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 855..868
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 878..891
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 898..901
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 903..905
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 910..915
FT /evidence="ECO:0007829|PDB:3HBL"
FT TURN 916..918
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 929..936
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 946..949
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 955..965
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 966..968
FT /evidence="ECO:0007829|PDB:3BG5"
FT HELIX 972..980
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 982..995
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 998..1000
FT /evidence="ECO:0007829|PDB:3HBL"
FT HELIX 1003..1008
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 1015..1021
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 1024..1033
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 1040..1048
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 1051..1058
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 1062..1064
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 1077..1081
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 1083..1091
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 1104..1112
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 1114..1118
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 1120..1128
FT /evidence="ECO:0007829|PDB:3HBL"
FT STRAND 1140..1145
FT /evidence="ECO:0007829|PDB:3HBL"
SQ SEQUENCE 1150 AA; 128558 MW; 2C8B9B7C1E7E3E48 CRC64;
MKQIKKLLVA NRGEIAIRIF RAAAELDIST VAIYSNEDKS SLHRYKADES YLVGSDLGPA
ESYLNIERII DVAKQANVDA IHPGYGFLSE NEQFARRCAE EGIKFIGPHL EHLDMFGDKV
KARTTAIKAD LPVIPGTDGP IKSYELAKEF AEEAGFPLMI KATSGGGGKG MRIVREESEL
EDAFHRAKSE AEKSFGNSEV YIERYIDNPK HIEVQVIGDE HGNIVHLFER DCSVQRRHQK
VVEVAPSVGL SPTLRQRICD AAIQLMENIK YVNAGTVEFL VSGDEFFFIE VNPRVQVEHT
ITEMVTGIDI VKTQILVAAG ADLFGEEINM PQQKDITTLG YAIQCRITTE DPLNDFMPDT
GTIIAYRSSG GFGVRLDAGD GFQGAEISPY YDSLLVKLST HAISFKQAEE KMVRSLREMR
IRGVKTNIPF LINVMKNKKF TSGDYTTKFI EETPELFDIQ PSLDRGTKTL EYIGNVTING
FPNVEKRPKP DYELASIPTV SSSKIASFSG TKQLLDEVGP KGVAEWVKKQ DDVLLTDTTF
RDAHQSLLAT RVRTKDMINI ASKTADVFKD GFSLEMWGGA TFDVAYNFLK ENPWERLERL
RKAIPNVLFQ MLLRASNAVG YKNYPDNVIH KFVQESAKAG IDVFRIFDSL NWVDQMKVAN
EAVQEAGKIS EGTICYTGDI LNPERSNIYT LEYYVKLAKE LEREGFHILA IKDMAGLLKP
KAAYELIGEL KSAVDLPIHL HTHDTSGNGL LTYKQAIDAG VDIIDTAVAS MSGLTSQPSA
NSLYYALNGF PRHLRTDIEG MESLSHYWST VRTYYSDFES DIKSPNTEIY QHEMPGGQYS
NLSQQAKSLG LGERFDEVKD MYRRVNFLFG DIVKVTPSSK VVGDMALYMV QNDLDEQSVI
TDGYKLDFPE SVVSFFKGEI GQPVNGFNKD LQAVILKGQE ALTARPGEYL EPVDFEKVRE
LLEEEQQGPV TEQDIISYVL YPKVYEQYIQ TRNQYGNLSL LDTPTFFFGM RNGETVEIEI
DKGKRLIIKL ETISEPDENG NRTIYYAMNG QARRIYIKDE NVHTNANVKP KADKSNPSHI
GAQMPGSVTE VKVSVGETVK ANQPLLITEA MKMETTIQAP FDGVIKQVTV NNGDTIATGD
LLIEIEKATD
