ID A0A0N0N0W5_9ACTN Unreviewed; 1082 AA.
AC A0A0N0N0W5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:KPI15331.1};
DE EC=5.1.1.13 {ECO:0000313|EMBL:KPI15331.1};
GN ORFNames=OK074_0039 {ECO:0000313|EMBL:KPI15331.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI15331.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI15331.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI15331.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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:KPI15331.1}.
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DR EMBL; LJCV01000111; KPI15331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0N0W5; -.
DR PATRIC; fig|1592327.3.peg.40; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0047689; F:aspartate racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR CDD; cd17652; A_NRPS_CmdD_like; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:KPI15331.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991}.
FT DOMAIN 1006..1081
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 982..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 118247 MW; 9EEC70AEE33B2208 CRC64;
MEDLHTRIAA LSPEHRALFE SRLRAAAGPG PDPGIPRRPD DGAPVPLSFA QHRIWFLDQL
EPSRAVYNVS ASLMLRRHLT TAVVRGALDE LTRRHEVLRT VFPSDDGEPR QRVMDRLSPP
LTETDLRELP ESDRAAAALS RCEENKRRPF DLASGPLLRC LLLRLRDDET LLFLTFHHTV
FDGWSIGVLR RDLTALLHAA ETGEASGLPA LPVQYADFAL WQRRQLDDRR LAELLGYWRE
RMRGAPPVID LPFDRPRPAV TTNEGAQRGF ALSAEVTAAL RELGTACGTT PFMTMLTLFA
ALLHRWSGEQ DMVIGTPVAN RARSELDDLI GFFTNNLAIR VGTGPGTSFR GLLAQVRQTT
VDALARQDLP FERLVEETRA ERTLTHNPLF QVVFVMEDGQ DAGELDTLVP EGHGETHTPG
SAKFDLTLTI TDSGSAFAGS FEYSTDLFEP VTIDRLTERL DLLARSVTAD PDLELAALPV
LTGDENRHLR QVNAAVEDDP PQHRTLHGVL EDAARRRPEN TAVEAPDRHL TYRQLDEAAN
RLAHYLLTLG VEAEQPIGVA LDETADAVVA AFGVLKAGAV LLPLDPAYPA ARLDHVLRRS
GAQLLLTRRS LADRFAGNDV TPVLMDDDTV RAALADQPGD RPAVSVPPQQ LAYVIFTSGS
TGVPKGVMVP HRGIGSLTRS FEQFAQGPGS RVLRFASPSF DASVMELLMT FGAGATLVLE
PRAELVPGED LARLIRERRI STVLLSPSAL STLTRSELPG LRTVVMGGEA ATLELAQQWC
DGRDVFNAYG PTEATICATI ARCSSGRVPP LGRPVAGCTL HVLDDTLSPV PFGRQGELYL
GGVGLARGYL AQPDVTAARF VPDPSGTEPG ARLYRTGDLV RWCADGELEF LGRADHQVKL
RGFRIEPGEI ETRLEDHPGV RTAVVLVRGE GADRRLVGYA VPAPGGERPT PADLRQWLKD
RLPGYMVPEL FVMLDALPTT PNGKLDRDAL PDPLERSQDT DRQRPPLLDP VEERVAEIWR
EVLGIALPGG ADNFFEVGGN SLSATRLVAR VNQVFGIRLP VRTLFVESTV SGLARSVAAA
RE
//
