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Database: UniProt
Entry: R7HQC5_9BACT
LinkDB: R7HQC5_9BACT
Original site: R7HQC5_9BACT 
ID   R7HQC5_9BACT            Unreviewed;       551 AA.
AC   R7HQC5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=AMP-binding enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN585_00445 {ECO:0000313|EMBL:CDE41496.1};
OS   Prevotella sp. CAG:279.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262924 {ECO:0000313|EMBL:CDE41496.1, ECO:0000313|Proteomes:UP000018375};
RN   [1] {ECO:0000313|EMBL:CDE41496.1, ECO:0000313|Proteomes:UP000018375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:279 {ECO:0000313|Proteomes:UP000018375};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDE41496.1}.
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DR   EMBL; CBIX010000113; CDE41496.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7HQC5; -.
DR   Proteomes; UP000018375; Unassembled WGS sequence.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR   GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR   PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018375}.
FT   DOMAIN          37..409
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          459..539
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   551 AA;  62571 MW;  18A422C87ED2F1FD CRC64;
     MLEKFLSKTK FDSYEDFMQN FKVNVPENFN FGYDVVDEWA RTNPDKPALL WTNEQGEKIQ
     FTFADIKRES DKAASFFTSL GIGRGDMVML ILKRRYQFWF SIIALHKIGA TTIPATHLLT
     AKDIVYRCQS ADIKAIVAVG DDIVLKHIDD ALPKCPSLKY RISTGPHIPE GWLDFNKGCA
     EAAPFVRPAE ANSNDDISLM YFTSGTTGEP KMVAHSFTYP LGHIITGSYW HNLHEDSLHL
     TLADTGWGKA VWGKLYGQWI AGANVFVYDF EKFKPVDVLQ MIHDHHITSF CAPPTVFRFL
     IREDLSKFDI SSLKYCTIAG EALNPSVYNE WLRLTGIKLM EGFGQTETTL TIATYPWLEP
     KPGSMGKKGP VYDIDLLTSD GRWAEDGEQG EIVVRTGDSR PLGLFKEYYR DPKLTHEAWH
     DGIYHTGDVA WRDEDGYYWF IGRKDDVIKS SGYRIGPFEV ESALMTHPAV VECAITGVPD
     EIRGQVVKAT IVLSKDYKDR ADEALVKDIQ DHVKRTTAPY KYPRVVEFVD ELPKTISGKI
     RRVEIRDKSK K
//
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