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}.
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; 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
//