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
//