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Database: UniProt
Entry: A0A150KKN9_9BACI
LinkDB: A0A150KKN9_9BACI
Original site: A0A150KKN9_9BACI 
ID   A0A150KKN9_9BACI        Unreviewed;      1196 AA.
AC   A0A150KKN9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:KYC90374.1};
DE            EC=6.2.1.3 {ECO:0000313|EMBL:KYC90374.1};
GN   ORFNames=B4102_3882 {ECO:0000313|EMBL:KYC90374.1};
OS   Heyndrickxia sporothermodurans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX   NCBI_TaxID=46224 {ECO:0000313|EMBL:KYC90374.1, ECO:0000313|Proteomes:UP000075666};
RN   [1] {ECO:0000313|EMBL:KYC90374.1, ECO:0000313|Proteomes:UP000075666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4102 {ECO:0000313|EMBL:KYC90374.1,
RC   ECO:0000313|Proteomes:UP000075666};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT   Foods.";
RL   Submitted (JAN-2016) 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:KYC90374.1}.
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DR   EMBL; LQYN01000128; KYC90374.1; -; Genomic_DNA.
DR   RefSeq; WP_066235526.1; NZ_LQYN01000128.1.
DR   AlphaFoldDB; A0A150KKN9; -.
DR   STRING; 46224.B4102_3882; -.
DR   PATRIC; fig|46224.3.peg.1025; -.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000075666; Unassembled WGS sequence.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd05235; SDR_e1; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
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; IPR042099; ANL_N_sf.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR44845:SF7; PLIPASTATIN SYNTHASE SUBUNIT D; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:KYC90374.1};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075666}.
FT   DOMAIN          711..785
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1196 AA;  134610 MW;  D2678FFBCA381C7A CRC64;
     MTKQINIKAS INEIINTLNF PVKQELKSTS NKFKTSLKNL PYTDNVLLVT AFISWIHRMT
     NEETVSLDIH KDGQFYPLEI TFSKETTVKT VVSVVQEALL KDGVEASTNH IIFTDKQIDD
     VEDIVFQLVV ERDNFYLAGA EQIINANFEQ RYLSSFNILA LDLNNNKEKA VLDLEILTPE
     EVVLWKSIND NKKDFPKGET LHGIFSKTAR NYPKKYALSN ESEKITFREL EKYSNQVANY
     LVTNGVKIGD YIAVYMERSI EAIVGMLGVM KAGAVYVPLS PDNPNERNAY IMQDANTKVV
     LTNRESMHLI DGVAPEDAQI MNIENIAGPA TPVHVDMKAT DIAYIIYTSG STGKPKGVKI
     PHKSIITFGY SELEIYDITS EDTLTQFYTL TFDASLLELC PMIFTGACLY MLSKEERLDV
     SLFADAIKRE NITSAMMLPM SALKQFSLYA TDKDVEAFRN LKYFGVGGEA LTGETARLFQ
     NRFGNIPLIN VYGPTECSVL STTYTVTDKI PEDLVNIPIG KPLKNYSVYI VNEKDHLNPI
     GVPGELLIET EGLSEGYLNL PEKTSEVFVK THLSDHLVYR SGDIVKLLDD GNIEFVGRKD
     SQVKIRGYRV EMGEIEDKLL QVDFIEDGAI VAADVNGDKI LVAYYKQKDN EIGSPKAVLD
     FLTTKVPKYM IPSYIIELED LPQLPSGKIN RKELAARPIE LKSSFDEDKK APSNEVEEKF
     VEAWKSVLGL SSVGVDENFF EIGGHSLKVL ATLSILKKDF PTLKINDFFT YPTIEALAQK
     IRHDQVVETE ENVFTNLKET DLYEHPKRLH TNLDYKAVSQ TGVLLTGVTG YLGSHILIDL
     VRDTNTTVYA LVRAKSREEG LERLKSTLSY YAPQNFYINY NLKDRVVVIP GDFTKADLGL
     SKEDYAKVQE KVNSIIHCGA DVRHFGSKEE FTKTNVDSTK NLLKLAEQLC NARFHYVSTL
     GIPEDLAMEG NWDRFLQATN IADAPEIMSL YTNSKLESEK LVEEYYKKGL PVTIYRPGNI
     TCQYETGMFQ MNINDNAVYR MLKGFILLGV APDVDYKMDF TMVDFASKSI TTIAMLDESI
     GGVYNICNPL NISYKEFIQS INDFGYDINL LPQQEYVDYL YSDQPKDKEG LELAMAGLEG
     DGAKDSPLVY TCPHTMSVLN KNGVKVPTPD KAFVFRMLEH AIHVGYFNRP AVLARV
//
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