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Database: UniProt
Entry: H0QXQ3_9ACTN
LinkDB: H0QXQ3_9ACTN
Original site: H0QXQ3_9ACTN 
ID   H0QXQ3_9ACTN            Unreviewed;      1538 AA.
AC   H0QXQ3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=Putative non-ribosomal peptide synthetase {ECO:0000313|EMBL:GAB17604.1};
GN   ORFNames=GOEFS_036_00430 {ECO:0000313|EMBL:GAB17604.1};
OS   Gordonia effusa NBRC 100432.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB17604.1, ECO:0000313|Proteomes:UP000035034};
RN   [1] {ECO:0000313|EMBL:GAB17604.1, ECO:0000313|Proteomes:UP000035034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB17604.1,
RC   ECO:0000313|Proteomes:UP000035034};
RA   Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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:GAB17604.1}.
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DR   EMBL; BAEH01000036; GAB17604.1; -; Genomic_DNA.
DR   RefSeq; WP_007316942.1; NZ_BAEH01000036.1.
DR   STRING; 1077974.GOEFS_036_00430; -.
DR   eggNOG; COG1020; Bacteria.
DR   OrthoDB; 2472181at2; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000035034; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 2.
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; SSF52777; CoA-dependent acyltransferases; 4.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035034}.
FT   DOMAIN          984..1058
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1538 AA;  165320 MW;  AEC436525F4103BE CRC64;
     MSQIEDVLAL SPLQEGLFSL AQLATERAGG EVPQGDVYTI PLVVDIDGPV DPEVLRRSLT
     ALLVRHPNLR AVFWDTDVPK PVQIVPSDIT LPWAERAVDA RGVDDATAAE VAKGFDLRRG
     PALRATLLTV GENRRRLIVT VHHILMDGWS LGVFFAELQA LYLAGGVATA LPPVRPYRDY
     IAWLADRDVA AVGQQWSDYL SGISAPLMVA EAASGSSIGA TAGARPVSTH YRLSTNDTAR
     LRDWARAQSI TLNTAAQFAW TLVLSRLVDR SDVVYGTIVT GRPERLPDAD RMIGLFLNTI
     PVAFTIDGQA TVVTECQRLQ RESTAMRDIG YLSLSAVQRA AGQGALFDAM FVFQNAPMEA
     AMGATDFGDG VTFTPVMGEN LTHYPLTVVS HLLGDELLIA VEAVASALPF TPDDLAASLL
     HVLRVLPDSA ASEVGDIDVV SVETRAQLAC AATTPALTAT EPETTIFSAF ERQVHATPHA
     LAIADDNTEL TYEEFYARVV RLAGELNTVG EEDVVAICLP RGIDSLVAIF AVLAAGAAYV
     PVDISLPASR IESIFAQAAP VASIVSGEGV AGLPRGELVI DLDDPKTVDR IAARPVESPR
     ARRDPAQAAY IIFTSGSTGE PKGVVNTNGA VVSYFADHRE RVYRPGRARL GRPLRIAHAW
     SLSFDASWQP MIGLLDGHAL QLFSEETMRD THRLVDGIAK FGVDMIDTTP SMFRQLEFAG
     VVDRGLTILA LGGEAIDAAL WARLRALPGV SVHNCYGPTE ATVEALVANL TVSQEFSDIS
     LANIGAPTAG MSGYILDSRL RQVPAGVVGE LYLAGPQVAR GYVGRPGTTA DRFVADPFVG
     ETSDGTGALS RRMYRTGDLV RRLRGGGIAY LGRSDDQVKI RGYRIEIGEV ETALRELPDV
     TAAAVAVVRR GGGAGLVGFT VGAELSPTLL RAQLGQRLPG YMIPARLLVL AELPVNSNGK
     TDVRELNRLA SEAMSTVGSN AGAVAATDTE RALVDLISEV FDGEAPGVED DFFELGLDSI
     VAISLATRAR KRGLAVTVRL IASYPTIRDL AAAVDLGLGE LADEDHDGYG DVMPLPYASW
     MFEQDNYRRF TQTVLLRVAD GATRADVESM LQAVLDGHDT LRSILVTNEN GETRQRTREP
     GTVFAASVLA EEEFEPAGPS NADRIAKVID RANEQMNPWA GELVRANLLR GGPSMDLLVL
     TIHHLAIDVV SWGVLMIDLS QAWEQIVAGE QPEPPTEITS YRRWCELMTE RADTPEVVAQ
     KEYWLSQVAT PDPALGAVVR GGVTWSSLRL AEVTINPSDS AALLAGVTRA DGVRELLLAA
     LTMALASWRI AHDTDHRQGS LIALVGHGRA DNALGTDTTG TAGWFTNVYP ARLGAGEFAV
     DLEEAERSPK RIAELVDSVV SHLASVPEQG LDYGLLRDIS RDQQIVAAAE PQVEFNYLGR
     FDHSGGPERP WTMVTDVELN RVIPLAPEPD MTLRFPLSLI AAVQAADDGQ PELATTVRWS
     DAVFTLAQID ELVDLWQRSV SLLATTRAAI EREKVCQP
//
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