ID   E5XP76_9ACTN            Unreviewed;      1188 AA.
AC   E5XP76;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   10-FEB-2021, entry version 59.
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}.
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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   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: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; 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 {ECO:0000213|PDB:5MSP, ECO:0000213|PDB:5MSR,
KW   ECO:0000213|PDB:5MSS, ECO:0000213|PDB:5MST};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450, ECO:0000256|PROSITE-
KW   ProRule:PRU00258}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004816}.
FT   DOMAIN          665..743
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
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
//