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Database: UniProt
Entry: A0A074MVN6_9SPHN
LinkDB: A0A074MVN6_9SPHN
Original site: A0A074MVN6_9SPHN 
ID   A0A074MVN6_9SPHN        Unreviewed;      1553 AA.
AC   A0A074MVN6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Peptide synthetase {ECO:0000313|EMBL:KEO99071.1};
GN   ORFNames=EH32_08185 {ECO:0000313|EMBL:KEO99071.1};
OS   Erythrobacter litoralis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=39960 {ECO:0000313|EMBL:KEO99071.1, ECO:0000313|Proteomes:UP000027866};
RN   [1] {ECO:0000313|EMBL:KEO99071.1, ECO:0000313|Proteomes:UP000027866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8509 {ECO:0000313|EMBL:KEO99071.1,
RC   ECO:0000313|Proteomes:UP000027866};
RA   Zheng Q.;
RT   "A comprehensive comparison of genomes of Erythrobacter spp. Strains.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:KEO99071.1}.
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DR   EMBL; JMIX01000003; KEO99071.1; -; Genomic_DNA.
DR   RefSeq; WP_034901660.1; NZ_JMIX01000003.1.
DR   KEGG; elq:Ga0102493_111355; -.
DR   PATRIC; fig|39960.10.peg.433; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000027866; Unassembled WGS sequence.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd08700; FMT_C_OzmH_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12230; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR024011; Biosynth_lucif-like_mOase_dom.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   NCBIfam; TIGR04020; seco_metab_LLM; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51679; Bacterial luciferase-like; 1.
DR   SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
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:UP000027866}.
FT   DOMAIN          1432..1508
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1505..1553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1535..1553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1553 AA;  167349 MW;  39137FFAD87F5464 CRC64;
     MTKFSSILIG NEALLVQCGE MLLRRGHTIG VVVTRTPPIA DWAQKNGIRV EKPGRSLAMR
     LGDVTVDWLF SIANLSLIPE DVLSLASKGA INFHDGPLPA YAGLNAPVWA LLNGERNHGI
     TWHMITDEVD AGEIVMRQAI AIDDDETAFT LNAKCFAAAI ESFGPLIEAL EVDNLSTEIQ
     DFSTRTIFAR ADRPHAAGRV DFKWSADRLA AFVRALDHGD YLNPLTTPKV DLGGFVASIR
     KAVQLPGGEA APGTVLAVEK DNILVATQGG SVRLSGLTDA TGAPVDPNQY TKAGAMLPAM
     DGADSLNAAL AQAAPRENAV RALLADPVPS DLGLSRPSKG TTAVGEIPIV VPDGLDRTRI
     VGVLAAAALR STHRDAIDIA YAGDPLPCSS GYMSDWVPVR IAVDRNVTMK ALAGDAHAQI
     DRARAHPSFA LDIVLRDPSI AAVAVPEFGI SEACEPGLIT GTAVTVHLSD TGLRMFHNGA
     RIDPDMAKLL AARIERLAAA IDYDAEIMLA SAPIMSDHEL ELVTRTWNQS EVNYDHDQTM
     HAAFEEQARR SPDAVALVFE GQELKYADLD TRANRVAHVL RDMGVAPGTF VGLYLNRSLD
     LVIAAIAILK AGGAYVPLDP AYPTDRTTLY IEDSGVKVIV TSAELAAHLP ESLAQTLLID
     RDEGIGAAAT DAPECAATGH DAAYLIYTSG STGRPKGVVL EHRNVMNFFR GMDDRVPHEP
     AGTWLALTSI SFDISVLELF YTLARGFKVV VVSEEARLNP SDGIARSDKG MQFSLFYWGN
     DDGVGPKKYE LLLEGAKFAD ANGFCAVWTP ERHFHAFGGP YPNPSVTGAA VAAVTKRIGV
     RAGSCVAPLH HSARIAEEWA VIDNLTDGRA GLAIASGWQP DDFLLRPENA PPNNKPAMLD
     AIETLRKLWR GEPVAFDHPL GGTIDVVTQP RPVSKDLPIW VTTAGNPDTW KEAGRIGANV
     LTHLLGQSIE EVAEKIGVYH AALREAGYDP AAHTVTLMLH TYLADSRDRA RETAREPMKD
     YLRSAAGLIK QYAWAFPAFK KPQGVTNPMQ IDLGSTNEEE MDAILEFAFS RYFEDSGLFG
     TIDDGVRRVE NLKAIGVNEI ACLIDYGIPV PQVIDGLAPL AEVLRQTNLD IELDDEDFSI
     AAQICRHEVT HLQCTPSMAR LLLADPGARE ALGRVEHLMI GGEALPGQLA RDLAGIVGRP
     IQNMYGPTET TIWSSTELTT GDEGTVNIGR PIVNTQFYVL DKDERPVPVG VPGELFIGGD
     GVAREYWKRP DLTAERFRPD PFVSPAGARI YRTGDLAKWR PDGRIDFLGR ADNQLKIRGH
     RIELGEIEAA LEEQATIRQA VVMAREDTPG DVRLVAYLLS DATISPVALR TALSAKLPDF
     MVPAHYIQVD AFPLTPNKKV DRKALPEPAE TAPLDKVTLA PKAISTPADA PAPSGNVEEQ
     IAAVWREVLG VSQIAPNDNF FSLGGHSLLA VQAHRELKAI FGPAKLSITD IFRFPTLGAL
     SQHLAPTPSG SGADDAAPVV QGAASEAGQG RGQMRKDAMS RRREMRARRK ESI
//
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