ID L8LS99_9CYAN Unreviewed; 1527 AA.
AC L8LS99;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Amino acid adenylation enzyme/thioester reductase family protein {ECO:0000313|EMBL:ELS00504.1};
GN ORFNames=Xen7305DRAFT_00002050 {ECO:0000313|EMBL:ELS00504.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS00504.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS00504.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS00504.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:ELS00504.1}.
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DR EMBL; ALVZ01000233; ELS00504.1; -; Genomic_DNA.
DR RefSeq; WP_006512445.1; NZ_ALVZ01000233.1.
DR STRING; 102125.Xen7305DRAFT_00002050; -.
DR PATRIC; fig|102125.3.peg.5365; -.
DR eggNOG; COG1020; Bacteria.
DR OrthoDB; 9757538at2; -.
DR Proteomes; UP000011203; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd19543; DCL_NRPS; 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; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
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; 2.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011203}.
FT DOMAIN 961..1035
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1527 AA; 173717 MW; 8596E8477B37A16B CRC64;
MATPTLTGFG LSPQQKRLWR LQQDDAAYLT QGAIAIAGNL QTARLKQVVE QIVARHQILR
TNFSRLPGVK LPVMTIADRS GFWWQEIDFR ERDLDLEELF EKESRQAYDL ETEASLRLAL
YQVSATNYIL KITLPALSAD YWTLKNLFNE IADGYGNYQA SQSAEEIQYV QFSEWQNQLL
SDEDATNAEK FWQEQRLNSF RLPFENHSVG VSRVKMQTLD IAIAEDLITQ LETIAQKYQT
KVSSILLACW QILIWRLTDE SSIAIGTYCD RREYEEMHSI MGLLATCLPI KSDLTGDLTF
AEVIANLEQT LESVLEWQDY FSLKSDDDLV FPIGFEFQEL PSPQDLGALT FSLLKQSSSI
ERHKLQLSGI RRQNSLFIEI NYDRGYFSPE TIDSLARQLQ ALLGSATTDP ECKIEELSIL
DARDRERIFH EFNQTTKDYP QGQSIQQLFA EQAQKTPHEI AVVFEEQQLT YAQLNSQANQ
LAHYLRERGV KPEVLVGLYL EKSSLSIVGL LGILKAGGAY LPLDANLPKA ALGDRLDDVQ
IVLTQQKLVS NLPQSIAEII CLDQDWQKIA KGSELDPSQE TSPENLTYVL FTSGSTGKPK
GVAIEQQQLL NYYYAICDRL HLQKNKSFAL VSSLAADLGN TVIFPALLTG GCLHLIANER
ASNPEALADY CDRHTIDYLK IVPSHLNALL SAAQPEKILP RKGLILGGET LSWQLVTKIQ
QYQPHCQIFN HYGPTETTVG VLTYQVETNT DHQSDTVPIG KPLANNQVYI LDKKLQPVPI
GVPGELYIAG AQVSRGYLNQ PELTAKKFIK NPLINIHLPS AFCHLPYLYK TGDRVRYLPN
GNIEFLGRID HQVKIRGYRI ELGEIEFALQ QHPQIKEAIA IARTDKTGKK RLVAYLVFEQ
QQSLNDQDLA NFLQQKLPNY MIPAVWIPLK ALPLTANGKV DRLALPAPEQ AKSQTEKVFV
APRNPTEAIL ADIWAQVLEV TQVSIDDNFF ELGGDSILSI QIIAKVNQAG FKATPKQIFE
YPTVAGLAAK ITPQDNNLNI EITSSAHDYK KFLPELQAKI APELLKSLED IYELTPIQKG
ILFHSLYDST NGLYLFQDTF TIKASLNIET FVAAWQQVVQ RHTILRTGFY WEDLEQPLQV
VYQQVKLPFD YQDWQNIETE KQQEQLQSFL KRDRSRNFDL AQPCPMRLTF FRLADDIYEL
VWTRHFIVAD GWSVPLLLNE VVQIYQSIEE KREFSLAPST PFRSYITWLN QQDPSQAKQF
WQQMLAGIKR PTPINNLYIE GNSDRQEQYD DRQIALSPTM SRQLNTFVKQ HHLTLNTLIQ
GVWAILLSHY SNQTEVLYGC TVSGRPPELE GVESIAGMLL NTLPVRVKVE PEKAILPWLK
QLQKLLVEIR QYEYSPLVEV KAWSEIPPGL PLFESIVVFE NLPQPESLRD EKRALEIIDF
NTFYKINYPI TVVVVPSFPL LVGVNYNFNL VDAGTIDGIL THFKMLLNFI MDNPDRCLQD
ISLVTKEQQK IIAMLEQQVT FNFDNSA
//
