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Database: UniProt
Entry: E9SEZ1_RUMAL
LinkDB: E9SEZ1_RUMAL
Original site: E9SEZ1_RUMAL 
ID   E9SEZ1_RUMAL            Unreviewed;      1764 AA.
AC   E9SEZ1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=AMP-binding enzyme {ECO:0000313|EMBL:EGC02121.1};
GN   ORFNames=CUS_5646 {ECO:0000313|EMBL:EGC02121.1};
OS   Ruminococcus albus 8.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC02121.1, ECO:0000313|Proteomes:UP000004259};
RN   [1] {ECO:0000313|EMBL:EGC02121.1, ECO:0000313|Proteomes:UP000004259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8 {ECO:0000313|EMBL:EGC02121.1,
RC   ECO:0000313|Proteomes:UP000004259};
RA   Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., Montgomery R.,
RA   Ziemer C., Klaassens E., Ocuiv P., Morrison M.;
RL   Submitted (FEB-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:EGC02121.1}.
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DR   EMBL; ADKM02000110; EGC02121.1; -; Genomic_DNA.
DR   RefSeq; WP_002851476.1; NZ_ADKM02000110.1.
DR   STRING; 246199.CUS_5646; -.
DR   eggNOG; COG0318; Bacteria.
DR   eggNOG; COG1020; Bacteria.
DR   OrthoDB; 9778383at2; -.
DR   Proteomes; UP000004259; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
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; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004259}.
FT   DOMAIN          1591..1666
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1675..1750
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          577..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1764 AA;  196364 MW;  F27A6F327C6B4A98 CRC64;
     MNEILDKIKD LTPEKRQRFM ALIEQDAEKY QIYPLSEEQE RMYFLYRSSP NDPYYNIVFA
     MGFGEKYSDE VIIKALRQLY SEQTMLRAVV MEAGDRIYQC IMKQDELPLT TVETDGAIWE
     KSCAEQLAHQ QVTPFDLNRA VPVRFTLISD GKRKKLITAV HHMFADNWSV GLICGRLRTL
     CAEICERGSF TEQSGGSYYD FIRWQKAAVF SADRDYWKEQ LNGCVQRIHL PKDGKDAKNG
     SNDSATAVAD LGAERSEKIR NAAKQAQVSV FSYLLTAFGL AMSAASGQSE VVVGTPVFNR
     VKEEFQRTVG CFANTIAVRM SFNDEYMLTH LRGTHKTVRE GLAHQSLPFN RVVDMVCEDR
     DPRITPLYQV MFNLESESVF GNQAQYAGDD ISMEIPDESR KVQFDLICGV MEREHIYQAG
     FVYRKELFSE ETANAVRDTF LDVIDAMLAD VQMSAESAAA EHKAWFAERS SAYAKKISKK
     LEERFSHACF DADIEDNCLM ISYVSSDSIP TEDMLETVSA YTDSPVIFIH AFSVGFIDDA
     QVRRQFAVMA QQEEAFRKNG AVQFARSEEH RQKWIWQDTE KKSSAEKSEA VDNDAPPSYM
     EGAPLAEIPY HTLADILLKA PAELMKNTIR TVQYGGAERE MTYAQLLENA RTAAASLNAM
     GLKKGSFAVL QMSDLYDCIT IFWGCQLAGI VAIPLGLPQG LEYRLNDAAT NKVWNVCRLL
     EDAYIIAGDK ETAGMEKFAA QTEPLCVRKM LRPSELYGGG KKGSYICEDV DEHDIAVMLF
     TSGSTGVPKG VMLDHHNIIK RSQGTSQRYG FDDKEVSLNW MPLDHVGGLV MYHILDVYDH
     ASQIQVETAE ILTDPLKWLK LIDRYRVSRT WAPNFAYGLV MEEQDKIPAL DVDLSCCKFI
     LNGGEAINFT ACDLFLKTLE QKGLAYSAMK PSWGMTETSS GILFSDRFGQ IVYRNSVTVG
     TPNDGVKAII ADEKGNAVPQ GAIGRLLVAG ETINRGYFRN EEENRKCFVD GGWFDTGDFA
     SVIDGEIVIT GRNKDIVIVN GVNITCLEVE KALEELDGIM SGGVACCGVR DEENVNDRVL
     ICFTKTDAVR DDLDGITKQM QNVLMRQFSI FADEYVALEE EQMPRTAIGK IDKKLLVKKY
     QAHEISGQRS VSGAGIKACM FTLERKSAPA GISGAESYLK FTQSGELPEE LPEKLYFVPS
     DDVSAEDIMA EISAIAKKLC DDRRDTVLLV RMPSYDTEKW ALVKGYLAAL PLEEAWVHTV
     LAVADEKTAE EQIVSEFSAR ENRYQQNRTV FFDGGVRKTE QLSAYMPDTQ SDWKKTWEGK
     TTVILGALGG VGSLFCEYLM KNCGGDYYLL GRGELSANSA KAAVYEKLTA IRPAKYLSCD
     ISVSGRLTEV LDAIEAESGT IDNIVNFTGD AGAVSHWESP EKHLIRNQNK ESIKQSMTVR
     RNAVDELAGY ASHSKETHIF ILSSITAVFG GYSFGGYSAV SSAQFYRFAS DPQFTVAASS
     KWHDIGMSSG EPEENYLLSE RLGFDTLRGE KSAEYLVKLF SVKPSAVMYG LNDHNYQILK
     SVNVHTGTSG FRADSKGAVL SGKVDAAAVS GGRASAAEKM RNIWIKTLKI DALADDDRFF
     EVGGNSLKSI NLVSRINEEF GTDLTVVDLF ENPTVRQLTD KAIEKGAAVG GGDADDMSGI
     CEELKHIWIK TLKIDKLSDD DRFFEVGGNS LKSINLVSRI NEKFKTELTV VDLFENPTVR
     QLSRIISENS AAARPAVSAK TFDI
//
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