ID E5XP76_9ACTN Unreviewed; 1188 AA. AC E5XP76; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 17-JUN-2020, entry version 55. 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; 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 945(T)= RT (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; NADP RP AND PHOSPHOPANTETHEINE. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 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 HOGENOM; CLU_009549_0_0_11; -. DR OrthoDB; 572620at2; -. DR BioCyc; GCF_000185725-HMP:HMPREF9336_RS16300-MONOMER; -. DR Proteomes; UP000004816; Unassembled WGS sequence. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. 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 InterPro; IPR036736; ACP-like_sf. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR InterPro; IPR042099; AMP-dep_Synthh-like_sf. 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}; Metal-binding {ECO:0000213|PDB:5MST}; KW NADP {ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, 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}. FT DOMAIN 665..743 FT /note="Carrier" FT /evidence="ECO:0000259|PROSITE:PS50075" FT NP_BIND 408..410 FT /note="AMP" FT /evidence="ECO:0000213|PDB:5MSS, ECO:0000213|PDB:5MST, FT ECO:0000213|PDB:5MSW" FT NP_BIND 429..430 FT /note="AMP" FT /evidence="ECO:0000213|PDB:5MSS, ECO:0000213|PDB:5MST, FT ECO:0000213|PDB:5MSW" FT NP_BIND 519..522 FT /note="AMP" FT /evidence="ECO:0000213|PDB:5MST, ECO:0000213|PDB:5MSW" FT NP_BIND 801..804 FT /note="NADP" FT /evidence="ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, FT ECO:0000213|PDB:5MSV" FT NP_BIND 868..869 FT /note="NADP" FT /evidence="ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, FT ECO:0000213|PDB:5MSV" FT NP_BIND 894..896 FT /note="NADP" FT /evidence="ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, FT ECO:0000213|PDB:5MSV" FT REGION 899..900 FT /note="Phosphopantetheine binding" FT /evidence="ECO:0000213|PDB:5MSV" FT REGION 1013..1018 FT /note="Phosphopantetheine binding" FT /evidence="ECO:0000213|PDB:5MSV" FT METAL 494 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000213|PDB:5MST" FT METAL 497 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000213|PDB:5MST" FT BINDING 315 FT /note="AMP" FT /evidence="ECO:0000213|PDB:5MST" FT BINDING 434 FT /note="AMP" FT /evidence="ECO:0000213|PDB:5MSS, ECO:0000213|PDB:5MST, FT ECO:0000213|PDB:5MSW" FT BINDING 507 FT /note="AMP" FT /evidence="ECO:0000213|PDB:5MSS, ECO:0000213|PDB:5MST, FT ECO:0000213|PDB:5MSW" FT BINDING 528 FT /note="AMP" FT /evidence="ECO:0000213|PDB:5MSS" FT BINDING 629 FT /note="AMP" FT /evidence="ECO:0000213|PDB:5MST" FT BINDING 702 FT /note="Phosphopantetheine" FT /evidence="ECO:0000213|PDB:5MSV" FT BINDING 828 FT /note="NADP" FT /evidence="ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, FT ECO:0000213|PDB:5MSV" FT BINDING 838 FT /note="NADP" FT /evidence="ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, FT ECO:0000213|PDB:5MSV" FT BINDING 934 FT /note="NADP; via carbonyl oxygen" FT /evidence="ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, FT ECO:0000213|PDB:5MSV" FT BINDING 970 FT /note="NADP" FT /evidence="ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, FT ECO:0000213|PDB:5MSV" FT BINDING 974 FT /note="NADP" FT /evidence="ECO:0000213|PDB:5MSR, ECO:0000213|PDB:5MSV" FT BINDING 997 FT /note="NADP" FT /evidence="ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR, FT ECO:0000213|PDB:5MSV" FT MOD_RES 702 FT /note="O-(pantetheine 4'-phosphoryl)serine" FT /evidence="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 //