CAR_SEGRC
ID CAR_SEGRC Reviewed; 1188 AA.
AC E5XP76;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Carboxylic acid reductase {ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000303|PubMed:28719588};
DE Short=CAR {ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000303|PubMed:28719588};
DE EC=1.2.1.- {ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588};
DE AltName: Full=ATP/NADPH-dependent carboxylic acid reductase {ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000305};
GN Name=car {ECO:0000255|HAMAP-Rule:MF_02247};
GN ORFNames=HMPREF9336_01297 {ECO:0000312|EMBL:EFV13858.1};
OS Segniliparus rugosus (strain ATCC BAA-974 / DSM 45345 / CCUG 50838 / CIP
OS 108380 / JCM 13579 / CDC 945).
OC Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae; Segniliparus.
OX NCBI_TaxID=679197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-974 / DSM 45345 / CCUG 50838 / CIP 108380 / JCM 13579 / CDC
RC 945;
RX PubMed=22675588; DOI=10.4056/sigs.2255041;
RA Earl A.M., Desjardins C.A., Fitzgerald M.G., Arachchi H.M., Zeng Q.,
RA Mehta T., Griggs A., Birren B.W., Toney N.C., Carr J., Posey J.,
RA Butler W.R.;
RT "High quality draft genome sequence of Segniliparus rugosus CDC 945(T)=
RT (ATCC BAA-974(T)).";
RL Stand. Genomic Sci. 5:389-397(2011).
RN [2] {ECO:0007744|PDB:5MSP, ECO:0007744|PDB:5MSR, ECO:0007744|PDB:5MSS, ECO:0007744|PDB:5MST, ECO:0007744|PDB:5MSV, ECO:0007744|PDB:5MSW}
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEXES WITH AMP; NADP AND
RP PHOSPHOPANTETHEINE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN,
RP PHOSPHOPANTETHEINYLATION AT SER-702, AND MUTAGENESIS OF HIS-900; TYR-966;
RP ASP-998; GLN-1015; ARG-1018 AND LEU-1131.
RX PubMed=28719588; DOI=10.1038/nchembio.2434;
RA Gahloth D., Dunstan M.S., Quaglia D., Klumbys E., Lockhart-Cairns M.P.,
RA Hill A.M., Derrington S.R., Scrutton N.S., Turner N.J., Leys D.;
RT "Structures of carboxylic acid reductase reveal domain dynamics underlying
RT catalysis.";
RL Nat. Chem. Biol. 13:975-981(2017).
CC -!- FUNCTION: Catalyzes the ATP- and NADPH-dependent reduction of
CC carboxylic acids to the corresponding aldehydes (PubMed:28719588).
CC Catalyzes the reduction of a very wide range of carboxylic acids,
CC including benzoic acids, heterocyclic, phenylacetic, phenylpropanoic
CC and fatty acid substrates (PubMed:28719588).
CC {ECO:0000269|PubMed:28719588}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylate + ATP + H(+) + NADPH = AMP + an aldehyde +
CC diphosphate + NADP(+); Xref=Rhea:RHEA:50916, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000255|HAMAP-Rule:MF_02247,
CC ECO:0000269|PubMed:28719588};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02247,
CC ECO:0000269|PubMed:28719588};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000255|HAMAP-
CC Rule:MF_02247, ECO:0000269|PubMed:28719588};
CC -!- DOMAIN: The N-terminal domain likely catalyzes substrate activation by
CC formation of an initial acyl-AMP intermediate, the central region
CC contains the phosphopantetheine attachment site, and the C-terminal
CC domain catalyzes the reduction by NADPH of the intermediate thioester
CC formed from the attack of the phosphopantetheine thiol at the carbonyl
CC carbon of acyl-AMP (By similarity). Large-scale domain motions occur
CC between the adenylation and thiolation states. Phosphopantetheine
CC binding alters the orientation of a key Asp, resulting in a productive
CC orientation of the bound nicotinamide. This ensures that further
CC reduction of the aldehyde product does not occur (PubMed:28719588).
CC {ECO:0000250|UniProtKB:Q6RKB1, ECO:0000269|PubMed:28719588}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC Carboxylic acid reductase subfamily. {ECO:0000255|HAMAP-Rule:MF_02247,
CC ECO:0000305}.
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DR EMBL; ACZI02000003; EFV13858.1; -; Genomic_DNA.
DR RefSeq; WP_007468889.1; NZ_KI391954.1.
DR PDB; 5MSP; X-ray; 2.41 A; A=1-1188.
DR PDB; 5MSR; X-ray; 2.37 A; A/B/C/D=1-1188.
DR PDB; 5MSS; X-ray; 1.96 A; A=1-1188.
DR PDB; 5MST; X-ray; 1.72 A; A/B=1-1188.
DR PDB; 5MSV; X-ray; 2.34 A; A/B/C/D=1-1188.
DR PDB; 5MSW; X-ray; 2.33 A; A=1-1188.
DR PDBsum; 5MSP; -.
DR PDBsum; 5MSR; -.
DR PDBsum; 5MSS; -.
DR PDBsum; 5MST; -.
DR PDBsum; 5MSV; -.
DR PDBsum; 5MSW; -.
DR AlphaFoldDB; E5XP76; -.
DR SMR; E5XP76; -.
DR STRING; 679197.HMPREF9336_01297; -.
DR EnsemblBacteria; EFV13858; EFV13858; HMPREF9336_01297.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG1022; Bacteria.
DR eggNOG; COG3320; Bacteria.
DR HOGENOM; CLU_009549_0_0_11; -.
DR OrthoDB; 572620at2; -.
DR Proteomes; UP000004816; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd05235; SDR_e1; 1.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR HAMAP; MF_02247; Carbox_acid_reduct; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR046407; CAR.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01746; Thioester-redct; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; NADP; Nucleotide-binding; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Reference proteome.
FT CHAIN 1..1188
FT /note="Carboxylic acid reductase"
FT /id="PRO_0000452836"
FT DOMAIN 665..743
FT /note="Carrier"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247"
FT BINDING 315
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MST"
FT BINDING 408
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSS,
FT ECO:0007744|PDB:5MST, ECO:0007744|PDB:5MSW"
FT BINDING 429..430
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSS,
FT ECO:0007744|PDB:5MST, ECO:0007744|PDB:5MSW"
FT BINDING 434
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSS,
FT ECO:0007744|PDB:5MST, ECO:0007744|PDB:5MSW"
FT BINDING 507
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSS,
FT ECO:0007744|PDB:5MST, ECO:0007744|PDB:5MSW"
FT BINDING 519..522
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MST,
FT ECO:0007744|PDB:5MSW"
FT BINDING 528
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSS"
FT BINDING 629
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MST,
FT ECO:0007744|PDB:5MSW"
FT BINDING 801..804
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSP,
FT ECO:0007744|PDB:5MSR, ECO:0007744|PDB:5MSV"
FT BINDING 828
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSP,
FT ECO:0007744|PDB:5MSR, ECO:0007744|PDB:5MSV"
FT BINDING 838
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSP,
FT ECO:0007744|PDB:5MSR, ECO:0007744|PDB:5MSV"
FT BINDING 868..869
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSP,
FT ECO:0007744|PDB:5MSR, ECO:0007744|PDB:5MSV"
FT BINDING 894..896
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSP,
FT ECO:0007744|PDB:5MSR, ECO:0007744|PDB:5MSV"
FT BINDING 934
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSP,
FT ECO:0007744|PDB:5MSR, ECO:0007744|PDB:5MSV"
FT BINDING 970
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSP,
FT ECO:0007744|PDB:5MSR, ECO:0007744|PDB:5MSV"
FT BINDING 974
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSR,
FT ECO:0007744|PDB:5MSV"
FT BINDING 997
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSP,
FT ECO:0007744|PDB:5MSR, ECO:0007744|PDB:5MSV"
FT MOD_RES 702
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02247,
FT ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSV"
FT MUTAGEN 900
FT /note="H->P,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28719588"
FT MUTAGEN 966
FT /note="Y->P: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28719588"
FT MUTAGEN 998
FT /note="D->G: Does not affect benzoic acid reduction rates
FT but leads to alcohol production. Displays modest
FT benzaldehyde reductase activity."
FT /evidence="ECO:0000269|PubMed:28719588"
FT MUTAGEN 1015
FT /note="Q->P: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28719588"
FT MUTAGEN 1018
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28719588"
FT MUTAGEN 1131
FT /note="L->Y: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28719588"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:5MST"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 67..79
FT /evidence="ECO:0007829|PDB:5MST"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 86..98
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 208..223
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:5MST"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:5MSS"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:5MST"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 343..350
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 359..376
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 383..394
FT /evidence="ECO:0007829|PDB:5MST"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:5MSW"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 413..423
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:5MST"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:5MST"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 450..456
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 472..479
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 490..495
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 503..513
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 516..522
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 537..544
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 550..556
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:5MSS"
FT STRAND 565..570
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 572..578
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 582..598
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 603..605
FT /evidence="ECO:0007829|PDB:5MST"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:5MST"
FT TURN 619..622
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 632..650
FT /evidence="ECO:0007829|PDB:5MST"
FT HELIX 656..661
FT /evidence="ECO:0007829|PDB:5MSS"
FT STRAND 666..668
FT /evidence="ECO:0007829|PDB:5MSS"
FT HELIX 670..681
FT /evidence="ECO:0007829|PDB:5MSS"
FT HELIX 686..688
FT /evidence="ECO:0007829|PDB:5MSW"
FT TURN 695..698
FT /evidence="ECO:0007829|PDB:5MSS"
FT HELIX 702..716
FT /evidence="ECO:0007829|PDB:5MSS"
FT HELIX 722..726
FT /evidence="ECO:0007829|PDB:5MSS"
FT HELIX 732..743
FT /evidence="ECO:0007829|PDB:5MSS"
FT HELIX 752..756
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 761..764
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 765..767
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 770..772
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 776..781
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 782..784
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 794..798
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 803..816
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 817..819
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 822..827
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 829..831
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 832..842
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 848..861
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 862..866
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 872..875
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 878..887
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 890..893
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 900..902
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 904..911
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 913..922
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 924..926
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 930..935
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 936..939
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 944..946
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 953..956
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 958..961
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 968..988
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 992..997
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 999..1001
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 1004..1006
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 1015..1026
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 1028..1031
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 1049..1051
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 1052..1064
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 1067..1075
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 1085..1094
FT /evidence="ECO:0007829|PDB:5MSV"
FT STRAND 1100..1104
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 1105..1117
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 1121..1126
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 1129..1135
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 1150..1159
FT /evidence="ECO:0007829|PDB:5MSV"
FT TURN 1162..1165
FT /evidence="ECO:0007829|PDB:5MSV"
FT HELIX 1172..1184
FT /evidence="ECO:0007829|PDB:5MSV"
SQ SEQUENCE 1188 AA; 128228 MW; 6E86BB01FEAB63D8 CRC64;
MTESQSYETR QARPAGQSLA ERVARLVAID PQAAAAVPDK AVAERATQQG LRLAQRIEAF
LSGYGDRPAL AQRAFEITKD PITGRAVATL LPKFETVSYR ELLERSHAIA SELANHAEAP
VKAGEFIATI GFTSTDYTSL DIAGVLLGLT SVPLQTGATT DTLKAIAEET APAVFGASVE
HLDNAVTTAL ATPSVRRLLV FDYRQGVDED REAVEAARSR LAEAGSAVLV DTLDEVIARG
RALPRVALPP ATDAGDDSLS LLIYTSGSTG TPKGAMYPER NVAQFWGGIW HNAFDDGDSA
PDVPDIMVNF MPLSHVAGRI GLMGTLSSGG TTYFIAKSDL STFFEDYSLA RPTKLFFVPR
ICEMIYQHYQ SELDRIGAAD GSPQAEAIKT ELREKLLGGR VLTAGSGSAP MSPELTAFIE
SVLQVHLVDG YGSTEAGPVW RDRKLVKPPV TEHKLIDVPE LGYFSTDSPY PRGELAIKTQ
TILPGYYKRP ETTAEVFDED GFYLTGDVVA EVAPEEFVYV DRRKNVLKLS QGEFVALSKL
EAAYGTSPLV RQISVYGSSQ RSYLLAVVVP TPEALAKYGD GEAVKSALGD SLQKIAREEG
LQSYEVPRDF IIETDPFTIE NGILSDAGKT LRPKVKARYG ERLEALYAQL AETQAGELRS
IRVGAGERPV IETVQRAAAA LLGASAAEVD PEAHFSDLGG DSLSALTYSN FLHEIFQVEV
PVSVIVSAAN NLRSVAAHIE KERSSGSDRP TFASVHGAGA TTIRASDLKL EKFLDAQTLA
AAPSLPRPAS EVRTVLLTGS NGWLGRFLAL AWLERLVPQG GKVVVIVRGK DDKAAKARLD
SVFESGDPAL LAHYEDLADK GLEVLAGDFS DADLGLRKAD WDRLADEVDL IVHSGALVNH
VLPYSQLFGP NVVGTAEVAK LALTKRLKPV TYLSTVAVAV GVEPSAFEED GDIRDVSAVR
SIDEGYANGY GNSKWAGEVL LREAYEHAGL PVRVFRSDMI LAHRKYTGQL NVPDQFTRLI
LSLLATGIAP KSFYQLDATG GRQRAHYDGI PVDFTAEAIT TLGLAGSDGY HSFDVFNPHH
DGVGLDEFVD WLVEAGHPIS RVDDYAEWLS RFETSLRGLP EAQRQHSVLP LLHAFAQPAP
AIDGSPFQTK NFQSSVQEAK VGAEHDIPHL DKALIVKYAE DIKQLGLL
