ID F4LIZ3_TREBD Unreviewed; 640 AA.
AC F4LIZ3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:AEE17302.1};
DE EC=6.2.1.3 {ECO:0000313|EMBL:AEE17302.1};
GN OrderedLocusNames=Trebr_1883 {ECO:0000313|EMBL:AEE17302.1};
OS Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE17302.1, ECO:0000313|Proteomes:UP000006546};
RN [1] {ECO:0000313|Proteomes:UP000006546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC {ECO:0000313|Proteomes:UP000006546};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Treponema brennaborense DSM 12168.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
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DR EMBL; CP002696; AEE17302.1; -; Genomic_DNA.
DR AlphaFoldDB; F4LIZ3; -.
DR STRING; 906968.Trebr_1883; -.
DR KEGG; tbe:Trebr_1883; -.
DR eggNOG; COG1022; Bacteria.
DR HOGENOM; CLU_000022_59_9_12; -.
DR OrthoDB; 311554at2; -.
DR Proteomes; UP000006546; Chromosome.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; PTHR43272:SF83; ACYL-COA SYNTHETASE LONG-CHAIN, ISOFORM J; 1.
DR PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:AEE17302.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006546}.
FT DOMAIN 33..414
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT REGION 610..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 69698 MW; 676E2B0196E811C7 CRC64;
MQTISDLGTY TFPALFRNTL LKFSECSALS MVHGTPITYR ELNARVERAA RLLYKNGFAP
KQKFAVFSSG MPNWGAAYLA IVNNGGIAVP LLPDFTAGEV EAILRHAEVD GMFVSDRLYA
RIESLAPELL PVVIKLDDFS VLRGGRAPAE TAAAEHAAAD NAQAADESAA PLPDVPVAET
DTASIIYTSG TTGRSKGVEL SHKNLVWTAI QCQTIHRVNK LDRCLSFLPL SHVYEFTIGF
AMQILNGSCV YYLEKPPTVS TLLPAFKLVR PTVVLSVPLI MEKIYKNKIV PTFTSKKLVA
RLYSIPLFRI LMNRAAGKQL KKTMGGKIKF FGIGGAKVDP EVERFMKEAR FPYAIGYGLT
ETSPLLAGSG PKETVPGTIG PVMEGVVMRI LDPDPRTGIG EVIACGPNVM RGYYRDEALT
EQAFTTAADS CGSGWFKTGD LGLLEKRKGR LWLSLKGRSK NMILGASGEN IYPEDIEFIL
NQHPLVSESL VVEDGNGLVA LVQLDEEKMK AEEKKRVAQP SAGKPAAGKP GLLPLPEVLQ
TAVENAAAAV SNAVEELKGD LLYKREEILS EIQFFINNKV NRISKIGKVE SVAQFEKTAS
QKIKRYLYNL KHGTHSPEGA PAPQNLRDSD ARDAADKNGN
//
