ID   E1KV40_FINMA            Unreviewed;      1715 AA.
AC   E1KV40;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=AMP-binding enzyme {ECO:0000313|EMBL:EFL55058.1};
GN   ORFNames=HMPREF9289_0862 {ECO:0000313|EMBL:EFL55058.1};
OS   Finegoldia magna BVS033A4.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=866773 {ECO:0000313|EMBL:EFL55058.1, ECO:0000313|Proteomes:UP000003807};
RN   [1] {ECO:0000313|EMBL:EFL55058.1, ECO:0000313|Proteomes:UP000003807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BVS033A4 {ECO:0000313|EMBL:EFL55058.1,
RC   ECO:0000313|Proteomes:UP000003807};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (AUG-2010) 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:EFL55058.1}.
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DR   EMBL; AEDP01000009; EFL55058.1; -; Genomic_DNA.
DR   Proteomes; UP000003807; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   PANTHER; PTHR45527:SF15; PYOCHELIN SYNTHASE PCHF; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          1290..1371
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1715 AA;  197612 MW;  00A75CF1FCF7C2C5 CRC64;
     MLRAIIYKNG KQKVQKDVPF VEIEENFSID EKELDLREKL ANKQYKIGEW PMCDIAITKI
     NEKTLLHFSV DMIVADYISM NIILKDLEDF YYNPEKEACN SSSYRDIVIY EKERKQNKSA
     NSQEDKKYWE NKIENMGNSP FLPTLKTVDI EDSSFLQKSI FLNEDMWSKL CDLSKNIGVT
     VSAVVMSVLS EIVYYWSGTN KFCINTTLFK RSSLNIKDIN EIVGDFTDVN VSAIDIDSKL
     TFKDRIINLQ KNLWMDMEHN SFSGVEVLRM LSRLKGENVV VPLVFTSTVG LSNENDVLLK
     RKVNYKISQT PQVYIDCQLA EEKTGARINW DIRKFVFDQV VMDEMFAGFV NIIKELCKNP
     YKILDLKNPV ELPENILQVR HDINSTQRKF PKRTLGDGFL KMLNKNPEKT ALIFKGNTYS
     YRKLSLYVSS IMEALKNNKI KSGDRIAVNI EKNEWQIASV LAIVLSGAVY VPIDVDQPIN
     RKNKILKKSD VKVVLSCDEE LSNSEFKNIN LHNISLSEFN SMKDLNLEKY YMDDAYIIFT
     SGTTGEPKGV RITHDAVMNT IIDVNERYRI KETDVFLGLA KLSFDLSVYD IFGCFDIGGT
     LVLPESEKTN DSKYIYDLML LHRVTIWNSV PAQMQLIVNY LEASEKIKKS EYLRLCMLSG
     DWIPTNLPSR VYNIFENVKL VSMGGATEAS IWSIYYNIGK NEKFDISVPY GYPMSNQKFF
     VLNRDLNPCP DYVKGGLYIG GKGISKGYIG DEKLNKEQFI RTRDGEIIYK TGDTGYYLKN
     GLIIFTGRES GDGQIKIHGY RIELSEIEDA IVSYNKVDSA QVVYTKGKSL DGKINAVVTP
     KIKSYISNDF YLGCDEIEFL KELESSVLEN MNLDLLIKWG NCADKVSLKS ILGTFQHFGI
     FTDQKSKYNI QEIKKIIKVP EKLEKLLKRW LNVLVKEKIL QLDEEQYQYL GEENGETLEQ
     LWNDFYKVEN EFNYSKDFLA YLKRSNDSLP ELITGIEDPL NLLFPKGDLK PALASYHDNK
     INRINNGFIA NEIHYLYNEN IKNSDKPFRI LEVGAGVGGT TIDVITKLKD SKVEYYFTDV
     SEFFFNNAKN IFHEYDWIKY KIFDINEDFY KQGLDAFSFD LILCANVLHN SRNIDFVIKN
     LKNLLVDSGT LIILEETKMS YMLLTSMEFK DGLIGFEDER KESEQTFFSK KQWEDIIDRN
     DGNITYAFPS SQLLEVSGQS VFVTRFKNEY YNIDKTELFE HLNDSLPNYM IPSDIKILQS
     LPKTSNGKIN KEEISSLFKV EDYDISIDKS QMTEIEKKIE HIWCKELNKS FIGLDENFYS
     VGGDSLLIAQ IISEILEKVE EAKDWDWSSL LTEMMQTPTI REISKKIQNR FDKIDKKIDK
     SLSVLKKSNL DNDKKTAKVL FHAGTGTLSA YTELLDYIIK DSNDVEDVLG FSFGDEAEYV
     SMKTEDTFKN LGEKYGEVLC KLGYSKYILI GHCVGGLIAI ETANYITNKN MNVSDVTLLS
     TTIPREQNRT VFHCLSRNKY DIALRTSLEN ELLLERTFSR LINADIFKAG HTVSDERLDD
     CIKYMVKNLD GDLKIESFER LVGEYEDIGL EFKRLSSIPI SERLNNLYNS INRDKLNLLD
     NEIRMLNTLF NIFSQNFGCV STYKPPKYSG NVRVFSCEET EKSFYGEFFG EDKETWEKYL
     AGNILYSSIS GQHFDCLTGE NLKQNSMKIL KFINE
//