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
//