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 29-MAY-2024, entry version 74. 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; Actinomycetota; Actinomycetes; Mycobacteriales; Segniliparaceae; OC 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}. 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; 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 eggNOG; COG0236; Bacteria. DR eggNOG; COG1022; Bacteria. DR eggNOG; COG3320; Bacteria. DR HOGENOM; CLU_009549_0_0_11; -. DR OrthoDB; 2472181at2; -. DR Proteomes; UP000004816; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:TreeGrafter. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:UniProtKB-UniRule. DR GO; GO:0031177; F:phosphopantetheine binding; IEA:UniProtKB-UniRule. DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt. DR CDD; cd17632; AFD_CAR-like; 1. DR CDD; cd05235; SDR_e1; 1. DR Gene3D; 1.10.1200.10; ACP-like; 1. DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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_com. 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 NCBIfam; NF041592; carboxyl_red; 1. DR NCBIfam; TIGR01746; Thioester-redct; 1. DR PANTHER; PTHR43272:SF52; CARBOXYLIC ACID REDUCTASE; 1. DR PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1. 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; SSF56801; Acetyl-CoA synthetase-like; 1. DR SUPFAM; SSF47336; ACP-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 //