ID A0A150UC83_9BRAD Unreviewed; 1181 AA.
AC A0A150UC83;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Thioester reductase {ECO:0000313|EMBL:KYG21779.1};
DE Flags: Fragment;
GN ORFNames=SE92_17270 {ECO:0000313|EMBL:KYG21779.1};
OS Bradyrhizobium sp. AT1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=574934 {ECO:0000313|EMBL:KYG21779.1, ECO:0000313|Proteomes:UP000075342};
RN [1] {ECO:0000313|EMBL:KYG21779.1, ECO:0000313|Proteomes:UP000075342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT1 {ECO:0000313|EMBL:KYG21779.1,
RC ECO:0000313|Proteomes:UP000075342};
RA Okubo T., Minamisawa K.;
RT "Evolution of nitrogen fixation genes.";
RL Submitted (JAN-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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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:KYG21779.1}.
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; JXDL01000001; KYG21779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150UC83; -.
DR STRING; 574934.SE92_17270; -.
DR PATRIC; fig|574934.3.peg.3650; -.
DR Proteomes; UP000075342; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd05926; FACL_fum10p_like; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
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; 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; IPR045310; Pcs60-like.
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; 2.
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; 2.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 533..608
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 1181
FT /evidence="ECO:0000313|EMBL:KYG21779.1"
SQ SEQUENCE 1181 AA; 128281 MW; 8E5CDFBD0666D741 CRC64;
MSDVTLPAPE KSSGTTAEAE MFACIGGLLD FYARKTPAAP ALLAPGRPIL NYGALGEVMQ
DLVRTLRRLG IAPADRIAVA LPRGADSALA LIAVASSGAC VPVNPDLTAD ELQRYFSELK
LTALVTRADM NSASRDVAKA LDIAVIDFVP GPQDNLGGCK FVGATVGPAA TGGASRGDDD
AFILLTSGTA ARPKMVPLTH RNVCLSATNA GRVLSLTSHD RLLNVLPLFH AHGLISGLLT
ALAAGSSVIC TDGFDAPSFF DWMRELRPTW YTAVPTIHRA LLTAAESDPD RARSSSLRVI
RSASASLAPT ILQGLEATFG VPVLETYGMT EAASQIAANP FDLRKVGSVG RAAGPEIAIM
DETGRALASG ERGEIMLRGP NMSRGYYNDE AATQAAFRDG WFRTGDLGYL DSDGYLFIVG
RIKDVINRGG QKISPIEVEE VLLSHPAVLE AGVFAVPHEK LGENVAAVVV LRSQAEATSE
QLRQFARKRL AAYKVPSLIR SVAALPKGGS GKVKRNALAE LIAKPESGDE ARLPRNALET
QLAAIWAGLL ELPRVSVDQD VFALGADSLA VTQMRSRLRE RFNVDFSFED IFDCATVAAL
AARLEAAANR REAALPAWRQ TREAEAPLSF QQQRMYVLSR LDPTRYNYNV VEVAVLKGLV
DVAALQASLA AICARHEALR SVIVERQGEP AQLVLQSPPR LERVKLKPCP ADKRAATIRR
EALKLAQHPF DLAHEPPLKV TLLSFDKTSH ALVVNVHHLV TDGWSQRLFW EELAAHYAAA
HRGSVAALPP PAFQYRDFAL WQQSWAQTPA AKDQLDYWRT QLDGVTTLPL RTDRPRPEIW
SGHGARHYLE FSRTLSAELR ALSQNQGVTP FMTLLAGFQC LLFRHTGHED VATGSLIANR
NQIESERLIG LFANTLILRN DFGGDPGFSE LLRRVRQVTL DAYRNQDLAI EEVLRALQIA
RRSDGNPLFR IMFILQNASI EAARFPGLSM RRLEIDPKVA RFDITLELVE ADGRFTGFFE
YATDLFDAAT IEAMAAQFKS LLKAVIADPE QRISRLPLLT EAERRQLLAT GRGVPANFTT
SGNLSERFDR QARTTPNAIA VTDGRASLSY RELARRSQAI ARLLVREGIG PESVVALLAD
RGPDLLAAMI GVQRAGAAFL NLDPDQPPAR LTTILGSSCA R
//
