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Database: UniProt
Entry: A0A3P2A5X6_9BACE
LinkDB: A0A3P2A5X6_9BACE
Original site: A0A3P2A5X6_9BACE 
ID   A0A3P2A5X6_9BACE        Unreviewed;       548 AA.
AC   A0A3P2A5X6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=AMP-binding protein {ECO:0000313|EMBL:RRD90266.1};
DE   SubName: Full=Putative long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:VFB13530.1};
DE            EC=6.2.1.- {ECO:0000313|EMBL:VFB13530.1};
GN   Name=fadK_1 {ECO:0000313|EMBL:VFB13530.1};
GN   ORFNames=EII33_08725 {ECO:0000313|EMBL:RRD90266.1}, NCTC7812_01056
GN   {ECO:0000313|EMBL:VFB13530.1};
OS   Bacteroides heparinolyticus.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=28113 {ECO:0000313|EMBL:RRD90266.1, ECO:0000313|Proteomes:UP000279562};
RN   [1] {ECO:0000313|EMBL:RRD90266.1, ECO:0000313|Proteomes:UP000279562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OH1047_COT-310 {ECO:0000313|EMBL:RRD90266.1,
RC   ECO:0000313|Proteomes:UP000279562};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:VFB13530.1, ECO:0000313|Proteomes:UP000396835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3012STDY7078512 {ECO:0000313|EMBL:VFB13530.1,
RC   ECO:0000313|Proteomes:UP000396835};
RG   Pathogen Informatics;
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; RQYF01000038; RRD90266.1; -; Genomic_DNA.
DR   EMBL; CAACYH010000004; VFB13530.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P2A5X6; -.
DR   OrthoDB; 9778383at2; -.
DR   Proteomes; UP000279562; Unassembled WGS sequence.
DR   Proteomes; UP000396835; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd05917; FACL_like_2; 1.
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; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 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   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:VFB13530.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279562}.
FT   DOMAIN          11..400
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          451..526
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   548 AA;  62227 MW;  24F241C0924C1A5B CRC64;
     MLYERTLGQW LEHWAETTPD KEYIVYSDRN LRFTWSRFNR RVDDMAKGLI AIGVQRGTHV
     GIWAANVPDW LTLLYACAKI GAVYVTVNTN YKQSELEYLC QNSDMHTLCI VNGEKDSDFV
     QMTYAMLPEL KTCERGHLKS ERFPHMKHVV YVGQEKHRGM YNTSELLVLG ENVEDDRLNE
     LKSQVTPHDV VNMQYTSGTT GFPKGVMLTH YNITNNGYLT GEHMKFTADD KLCVCVPLFH
     CFGVVLATMN CLTHGCMQVM VERFDPLVVL ASIHKERCTA LYGVPTMFIA ELHHPMFDMF
     DMSSLRTGIM AGALCPIELM KQVEEKMFMK VTSVYGLTEA SPGMTATRID DSFEVRCNTV
     GSDFEHTEVR VINPETGEEC PVGVQGEMCN RGYNTMKGYY KNPEATAEVI DKNGFLHSGD
     LGVKDENGNY RITGRIKDMI IRGGENIYPR EIEEFLYQLK GIKDVQVAGI PSKKYGEAVG
     AFIILREGAD LHESDVRDFC IGKISRYKIP KYIFFVKEFP MTGSGKIQKF KLKDLGLQLC
     KEQGIEII
//
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