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Database: UniProt
Entry: A8UNR2_9FLAO
LinkDB: A8UNR2_9FLAO
Original site: A8UNR2_9FLAO 
ID   A8UNR2_9FLAO            Unreviewed;      1334 AA.
AC   A8UNR2;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Amino acid adenylation {ECO:0000313|EMBL:EDP70118.1};
GN   ORFNames=FBALC1_11312 {ECO:0000313|EMBL:EDP70118.1};
OS   Flavobacteriales bacterium ALC-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP70118.1, ECO:0000313|Proteomes:UP000003630};
RN   [1] {ECO:0000313|EMBL:EDP70118.1, ECO:0000313|Proteomes:UP000003630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALC-1 {ECO:0000313|EMBL:EDP70118.1,
RC   ECO:0000313|Proteomes:UP000003630};
RA   Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) 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:EDP70118.1}.
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DR   EMBL; ABHI01000004; EDP70118.1; -; Genomic_DNA.
DR   STRING; 391603.FBALC1_11312; -.
DR   eggNOG; COG1020; Bacteria.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000003630; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0019752; P:carboxylic acid metabolic 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; 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; 3.40.50.1820; 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; 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   InterPro; IPR006162; Ppantetheine_attach_site.
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; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 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.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003630}.
FT   DOMAIN          979..1054
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   COILED          492..519
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1334 AA;  150623 MW;  925135E840D63E34 CRC64;
     MKPPTITKNN IYFNPFIGGP TIEKVIYTTQ SQVEIWIDCK IGGEDANRAY NESISLILEG
     ELSISALENA VQKLVKRHEA LRAVFSPDGR FMSVLHYVPV EIEHLNFSQS SSSNIKSTLS
     NYLLDDVNYI FDLVKGPLFK VGLIKINDLE HQLIITAHHI ICDGWSVGVI LEELGALYSA
     SVTNVNPSLP KVDDFSSYAD ELHAYIGSEA HLKTEKFWLD QYKTSVPKLT LPTDFSRPKL
     RTYKSNRLDF SINKEVISRL KKVGVKSGCS FVTTLMAAFE VFLFKQSGQD DIVLGLPSAG
     QSVTGKTQLI GHCVNLLPLR SKLDASQSFS EYLKHRKLSI LDAYDHQQLS FGELLQILPL
     RRDPSRVPLV PVVFNIDIGM TSQVKFTNLK YKLITNPRTF EAFELFLNAS GTEEDFILEW
     SYNSTLFTSS TIKQMMVTFE EILDLIIENS THTIAEIIKI DEAAYNQLND TEAIYPNLPL
     HELLSKQAKV FYKKQAIKFD ETEISYEKLE QQVNQLAHRL SSIGVSAGDF VGVCLSRSIE
     LVITLRAIMQ CGAAYIPLDP SYPLQRLNYM LDDSESKFLI STSIVSSKLS TNATVLILDD
     LFLNLSDFPK KPISIKVDPE DIAYLIYTSG STGKPKGVAV THKNLVNFLY SMMEKPGIKE
     TDRLLSITTI SFDIVGLELF LPLLSGATLV LANDETVKDG RIMLDLIKDE GVTILQATPT
     TWQMLLDIGW NIALPIKALS GGEPLSLSLS KRLLANVSEL WNMYGPTETT IWSSTKQILR
     DEDVITIGNP IANTQVYILN EQNILMEPGK TGEIVIGGDG VSEGYWKRLD LTNEKFFNNP
     FAIDSNTKLF RTGDLGQLLP SGELLCLGRI DHQVKVRGHR IELEEIERII DVLDDVNHSL
     VIVKADNLIA YIISEKIDEL SKDQVNQWKK AIAEQLPTYM IPQEFHLISE FPMTLNGKVD
     RNALLNKSTT QVHIANYTSP RNETEHIISE IWCEALNMEK IDVYSNFFEL GGHSIIAIKV
     ISQIENKMGE ILPLSALMVY PTIEKLASSI DRSVKKQSLG SLVPLKPEGT KTPLYIVHGA
     HFDVYLFNDL ARELDEDQPV YAIQPKGLNG IDEPLDSIYE MAAYYIAKME ISNPDGPYAL
     AGFSMGGIIA YEMAKQLKAK GKKVTMLASF DSYVYPSYFY NNTTKKKIVS FFYSISQMIF
     ISLNMFSSKK NFKRRIKLSK QYIYGLYLRL KVGRERQFKL QHNRTLKMNK KHIIATYQYT
     MMPEDIVVDL FKAKENVFFA HDFKFLGWKK FALKGVRKHM VPGNHVDMFV SPNVEVYASN
     LQRVLDNSNL ESFE
//
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