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Database: UniProt
Entry: A0A0D6KDU2_9CYAN
LinkDB: A0A0D6KDU2_9CYAN
Original site: A0A0D6KDU2_9CYAN 
ID   A0A0D6KDU2_9CYAN        Unreviewed;      1093 AA.
AC   A0A0D6KDU2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=AMP-binding enzyme {ECO:0000313|EMBL:EKE97866.1};
GN   ORFNames=FDUTEX481_04672 {ECO:0000313|EMBL:EKE97866.1};
OS   Tolypothrix sp. PCC 7601.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1188 {ECO:0000313|EMBL:EKE97866.1, ECO:0000313|Proteomes:UP000032761};
RN   [1] {ECO:0000313|EMBL:EKE97866.1, ECO:0000313|Proteomes:UP000032761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX   PubMed=25953173;
RA   Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA   Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA   Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA   Kehoe D.M., Weinstock G.M.;
RT   "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT   Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT   PCC 7601.";
RL   Genome Announc. 3:0-0(2015).
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:EKE97866.1}.
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DR   EMBL; AGCR01000109; EKE97866.1; -; Genomic_DNA.
DR   RefSeq; WP_045873881.1; NZ_JH930372.1.
DR   AlphaFoldDB; A0A0D6KDU2; -.
DR   STRING; 1188.FDUTEX481_04672; -.
DR   PATRIC; fig|1188.3.peg.8658; -.
DR   HOGENOM; CLU_000022_2_4_3; -.
DR   OrthoDB; 9757538at2; -.
DR   Proteomes; UP000032761; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd12117; A_NRPS_Srf_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; IPR009081; PP-bd_ACP.
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   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.
PE   4: Predicted;
FT   DOMAIN          996..1071
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1093 AA;  121785 MW;  265EBE1AE299815A CRC64;
     MTLSPVNFQS ELTAVEFDPF AEGELLLTAP ATESQKEIWA SVQMGDAANC AYNESQSLRF
     KGKLDVTVFQ SALQELVLRH EALRTTFSTD GNTLCIVDSL QIEIPIIDIS SLEPQEQQEK
     LASIRIQEVE KPFDLEHGPL FRAQIIKLQP QEHIAILTAH HIICDGWSWA VLMPDLGKLY
     SGLLEGIVPE LDESDRLSDY AVLQEEEVDS PEAIATEQYW LEQFADSVPV LDFPCDRPRP
     HIRTFNAARE DWQLNPQLVA DLKQLGTKFG CSFMTTILAG FEAWLHRITG QNDLVVGIPA
     AGQAALGQYN LVGHCVNLLP LRSQINGAQS FSEYLQSRRS TVLDAYDHQQ FTFGSLVKKL
     SIPRDSSRIP LVPITFNIDQ GLDSDKLPFS GLEVEFFSNP RSFENFELFI NATELRGQLT
     LECQYNTNLF DADTIHRRMA EFETLLQGIV ANPNQTIAKL PILPAVEQQL LAAWNQTQTN
     YPQDQSIHQL FEEQVARTPD AVALVFQGQQ LTYQELNTRA NQLAQYLQTL GVGADVLVGI
     CVERSLEMIV GLLGILKAGG AYVPLDPGYP QERLAFMLAD TQIKLLVTQK RLVEKLPTHN
     ANVICLDADW HTISQQAAEN LITNVKPHNL AYVMYTSGST GQPKGVSVIH QGVVRLVKET
     NYVSLTEKEI FLQISPVSFD ASTFEIWGCL LNGGKLVIFP PHTPSLDELG GIIQQYQVTT
     LWLTAGLFHL IVDEKIEALK PLRQLLAGGD VLSVPHVQKF LNTVENCKLI NGYGPTESTT
     FTSCYEITAP LKPGVSIPIG RPIANTQVYI LDSHLQQVPI GITGELYIGG DGLAREYFNR
     PDLTAERFIA NPLSADSQSR LYKSGDLARY LPNGEIEYLG RIDNQVKVSG FRIELGEIEI
     ALLQSPLVKE AVVIVREDSP GEKLLVGYFV AETNEDSSQI ISELRRFLKQ QLPEYMVPKI
     FVALEALPLN ANGKVDRRAL PKPDAYSPEL EANYVAPRTP IEQKISDIWT QVLNVKRVGI
     YDNFFELGGY SLLGIQVISR LRQALQVEIL MSNLFELPTV ADLAERVETL RWATQGIEGA
     ESDSADDYEE GEL
//
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