ID E5XP76_9ACTN Unreviewed; 1188 AA. AC E5XP76; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-JAN-2019, entry version 44. DE SubName: Full=Thioester reductase domain-containing protein {ECO:0000313|EMBL:EFV13858.1}; GN ORFNames=HMPREF9336_01297 {ECO:0000313|EMBL:EFV13858.1}; OS Segniliparus rugosus ATCC BAA-974. OC Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae; OC Segniliparus. OX NCBI_TaxID=679197 {ECO:0000313|EMBL:EFV13858.1, ECO:0000313|Proteomes:UP000004816}; RN [1] {ECO:0000313|EMBL:EFV13858.1, ECO:0000313|Proteomes:UP000004816} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-974 {ECO:0000313|EMBL:EFV13858.1, RC ECO:0000313|Proteomes:UP000004816}; 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 RT 945(T)= (ATCC BAA-974(T))."; RL Stand. Genomic Sci. 5:389-397(2011). RN [2] {ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, ECO:0000213|PDB:5MSS} RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH AMP; CALCIUM; RP NADP AND PHOSPHOPANTETHEINE. RX PubMed=28719588; DOI=10.1038/nchembio.2434; RA Gahloth D., Dunstan M.S., Quaglia D., Klumbys E., RA Lockhart-Cairns M.P., Hill A.M., Derrington S.R., Scrutton N.S., RA Turner N.J., Leys D.; RT "Structures of carboxylic acid reductase reveal domain dynamics RT underlying catalysis."; RL Nat. Chem. Biol. 13:975-981(2017). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV13858.1}. 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 ProteinModelPortal; E5XP76; -. DR SMR; E5XP76; -. DR STRING; 679197.HMPREF9336_01297; -. DR EnsemblBacteria; EFV13858; EFV13858; HMPREF9336_01297. DR eggNOG; ENOG4105E4E; Bacteria. DR eggNOG; COG1022; LUCA. DR eggNOG; COG3320; LUCA. DR OrthoDB; 572620at2; -. DR Proteomes; UP000004816; Unassembled WGS sequence. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; 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 InterPro; IPR036736; ACP-like_sf. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR InterPro; IPR013120; Male_sterile_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 {ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, KW ECO:0000213|PDB:5MSS, ECO:0000213|PDB:5MST}; KW Calcium {ECO:0000213|PDB:5MST}; KW Complete proteome {ECO:0000313|Proteomes:UP000004816}; KW Metal-binding {ECO:0000213|PDB:5MST}; KW NADP {ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, KW ECO:0000213|PDB:5MSV}; KW Nucleotide-binding {ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, KW ECO:0000213|PDB:5MSS, ECO:0000213|PDB:5MST}; KW Phosphopantetheine {ECO:0000213|PDB:5MSV, ECO:0000256|PROSITE- KW ProRule:PRU00258}; KW Reference proteome {ECO:0000313|Proteomes:UP000004816}. FT DOMAIN 665 743 Carrier. {ECO:0000259|PROSITE:PS50075}. FT NP_BIND 408 410 AMP. {ECO:0000213|PDB:5MSS, FT ECO:0000213|PDB:5MST, ECO:0000213|PDB: FT 5MSW}. FT NP_BIND 429 430 AMP. {ECO:0000213|PDB:5MSS, FT ECO:0000213|PDB:5MST, ECO:0000213|PDB: FT 5MSW}. FT NP_BIND 519 522 AMP. {ECO:0000213|PDB:5MST, FT ECO:0000213|PDB:5MSW}. FT NP_BIND 801 804 NADP. {ECO:0000213|PDB:5MSP, FT ECO:0000213|PDB:5MSR, ECO:0000213|PDB: FT 5MSV}. FT NP_BIND 868 869 NADP. {ECO:0000213|PDB:5MSP, FT ECO:0000213|PDB:5MSR, ECO:0000213|PDB: FT 5MSV}. FT NP_BIND 894 896 NADP. {ECO:0000213|PDB:5MSP, FT ECO:0000213|PDB:5MSR, ECO:0000213|PDB: FT 5MSV}. FT REGION 899 900 Phosphopantetheine binding. FT {ECO:0000213|PDB:5MSV}. FT REGION 1013 1018 Phosphopantetheine binding. FT {ECO:0000213|PDB:5MSV}. FT METAL 494 494 Calcium; via carbonyl oxygen. FT {ECO:0000213|PDB:5MST}. FT METAL 497 497 Calcium; via carbonyl oxygen. FT {ECO:0000213|PDB:5MST}. FT BINDING 315 315 AMP. {ECO:0000213|PDB:5MST}. FT BINDING 434 434 AMP. {ECO:0000213|PDB:5MSS, FT ECO:0000213|PDB:5MST, ECO:0000213|PDB: FT 5MSW}. FT BINDING 507 507 AMP. {ECO:0000213|PDB:5MSS, FT ECO:0000213|PDB:5MST, ECO:0000213|PDB: FT 5MSW}. FT BINDING 528 528 AMP. {ECO:0000213|PDB:5MSS}. FT BINDING 629 629 AMP. {ECO:0000213|PDB:5MST}. FT BINDING 702 702 Phosphopantetheine. {ECO:0000213|PDB: FT 5MSV}. FT BINDING 828 828 NADP. {ECO:0000213|PDB:5MSP, FT ECO:0000213|PDB:5MSR, ECO:0000213|PDB: FT 5MSV}. FT BINDING 838 838 NADP. {ECO:0000213|PDB:5MSP, FT ECO:0000213|PDB:5MSR, ECO:0000213|PDB: FT 5MSV}. FT BINDING 934 934 NADP; via carbonyl oxygen. FT {ECO:0000213|PDB:5MSP, ECO:0000213|PDB: FT 5MSR, ECO:0000213|PDB:5MSV}. FT BINDING 970 970 NADP. {ECO:0000213|PDB:5MSP, FT ECO:0000213|PDB:5MSR, ECO:0000213|PDB: FT 5MSV}. FT BINDING 974 974 NADP. {ECO:0000213|PDB:5MSR, FT ECO:0000213|PDB:5MSV}. FT BINDING 997 997 NADP. {ECO:0000213|PDB:5MSP, FT ECO:0000213|PDB:5MSR, ECO:0000213|PDB: FT 5MSV}. FT MOD_RES 702 702 O-(pantetheine 4'-phosphoryl)serine. FT {ECO:0000256|PROSITE-ProRule:PRU00258}. 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 //