ID K9PTF2_9CYAN Unreviewed; 1348 AA.
AC K9PTF2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:AFY36084.1};
DE EC=5.1.1.3 {ECO:0000313|EMBL:AFY36084.1};
GN ORFNames=Cal7507_5764 {ECO:0000313|EMBL:AFY36084.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY36084.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY36084.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY36084.1,
RC ECO:0000313|Proteomes:UP000010390};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003943; AFY36084.1; -; Genomic_DNA.
DR RefSeq; WP_015131873.1; NC_019682.1.
DR STRING; 99598.Cal7507_5764; -.
DR KEGG; calo:Cal7507_5764; -.
DR PATRIC; fig|99598.3.peg.6459; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3319; Bacteria.
DR HOGENOM; CLU_000022_2_13_3; -.
DR OrthoDB; 9757538at2; -.
DR Proteomes; UP000010390; Chromosome.
DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; 3.40.50.1820; alpha/beta hydrolase; 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; IPR029058; AB_hydrolase.
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; IPR001031; Thioesterase.
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 Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:AFY36084.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010390}.
FT DOMAIN 998..1073
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1348 AA; 151710 MW; C14367C36E807B23 CRC64;
MKIVATKDLY QLSSMQQGML FNNLVAQNSG VDIEQMICLV DEKIDVLAFQ QAWQTVVARH
AVLRTSFDWE SEREPQQRVH RNVIIPLEQQ DWCDLSDTEQ STKLQAYLQS DRRRGFQLND
APLMRLALFR LQESVYQFIW TFHHALLDGR SLSVIIKELF TLYDAFCEGK DLQLPQPHPY
QDHIAWLHQQ DWNKAESFWR DLLKGLTAPT PLLVDSVPRE QGSFGEQAIR LSEKTTAMLQ
SLAQQHQLTL NTLVQGAWAL LLSRYSGETD VVFGATRACR HSSVAGAESM VGLLINTLPV
RVSVSGEKPL LTWLRELRSQ WLALRDYEHT PLVKIQRWSD VPGGTSLFDS ILVFENYELN
SALRSQGGRW QNLEFQLEEQ TNFPLTLVGY AESELLLKLK YDQKKFADAK IRRMLGHLQT
LLSSMATNPW QYLGELPLLT TDEKHQMLIE WNHTQADFAE QLCIHQLFEA QVEQTPDAIA
VVCGEEQLTY KDLNCRANQL AHHLQQLGVK PGVLVAVYLE RSLEMIPAVL GILKAGGAYV
PLEPSFPKAR IQLLLSSGQI NCLVTQTCLL PSIYELELIA LQHLICLDQS AHTQSVQQVG
HQQVWNRAYL DLLPTKNLPK SANSNDIAYV IFTSGSTGTP KGVVVRHQPV INLIEWVNKT
FNVNADDRVL FITSLCFDLS VYDIFGLLAA GGSIRVVASH DVRDPEALLD ILCHEPITFW
DSAPPALQQL ATFFPMVHES NCHPQLRLVF MSGDWIPVPL ADLLKTTFPG VEVISLGGAT
EATVWSNYYP IGKVEPYWKS IPYGKPIQNA EYYILDAYLN PCPIGVSGEL HIGGECLASG
YLNQPELTAQ KFIPNPFSDK REARLYKTGD LARYLSDGNI EFLGRIDHQV KIRGFRIELG
EIESVLTQHN CVQETVVIAR EDEPGNKRLV AYVVVNGEST PTMNELRRFL QEKLPEYMIP
SAFVAIAHIP LTPNGKVDRR ALPIPNQTRS ELEKAFVAPK NTVEIELAQI WSAVLGIESI
GISDHFFDLG GNSLLAVKLF TQIEKKFGQK LPLATLFQAP TIEQLASILS QSHQSASWSS
LVTIQPSSNA KRPLFLIHAL GGNVIGYQTL VRYLGSEQPV YGLQAQGLDG KQAPHTRVED
MASHYIQEIR TVQPHGPYML GGFSSGGTVA FEMARQLVAQ GDRVALLAMF DTYSPSLYIN
HPSLVRTLYV YLLTFLRLRS PDRWNYFFAK VDWFKSMLTG KPSSKFDLWN EHSFAEDANP
YNMVLIEALK QATMADYLPQ PYAGKVTLFT TKEVLRWCQF QPCRGWNGMA KKGVEIHEVP
GTHLGMLGEP SVQTLAEKLI VCLEQAQG
//
