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Database: UniProt
Entry: A0A0B2JZ43_9FIRM
LinkDB: A0A0B2JZ43_9FIRM
Original site: A0A0B2JZ43_9FIRM 
ID   A0A0B2JZ43_9FIRM        Unreviewed;       494 AA.
AC   A0A0B2JZ43;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Long-chain fatty acid--CoA ligase {ECO:0000313|EMBL:KHM52804.1};
GN   ORFNames=NZ47_02430 {ECO:0000313|EMBL:KHM52804.1};
OS   Anaerovibrio lipolyticus.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Anaerovibrio.
OX   NCBI_TaxID=82374 {ECO:0000313|EMBL:KHM52804.1, ECO:0000313|Proteomes:UP000030993};
RN   [1] {ECO:0000313|EMBL:KHM52804.1, ECO:0000313|Proteomes:UP000030993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5S {ECO:0000313|EMBL:KHM52804.1,
RC   ECO:0000313|Proteomes:UP000030993};
RX   PubMed=23950883;
RA   Prive F., Kaderbhai N.N., Girdwood S., Worgan H.J., Pinloche E.,
RA   Scollan N.D., Huws S.A., Newbold C.J.;
RT   "Identification and characterization of three novel lipases belonging to
RT   families II and V from Anaerovibrio lipolyticus 5ST.";
RL   PLoS ONE 8:E69076-E69076(2013).
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:KHM52804.1}.
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DR   EMBL; JSCE01000046; KHM52804.1; -; Genomic_DNA.
DR   RefSeq; WP_039206113.1; NZ_JSCE01000046.1.
DR   AlphaFoldDB; A0A0B2JZ43; -.
DR   STRING; 82374.NZ47_02430; -.
DR   eggNOG; COG0318; Bacteria.
DR   Proteomes; UP000030993; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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:KHM52804.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030993}.
FT   DOMAIN          11..353
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          403..478
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   494 AA;  55168 MW;  550BCCFF5E35987F CRC64;
     MLIHDLVYRG KDDAVAVIDK ERTFTYKDLQ NSVKEYRNYL YNIGVRRGDR VGIFSRNNSD
     ILLAYMAIVS LGALAVPINF QLSNREIAYI VKDAGIIHVL TYKELDIAEA LDELHFTENV
     QQHNLRYCYQ EQSCPDAPKL PDDFKDTEPC VIIYTSGTTG NPKGAVLCHR NIIANDEQYH
     EVAHGTSDLV ELCVLPMYHC FGWTLSVMYP LYVGGKMVIL DKFTPKETIE TIREYGITDT
     HVVPSICALL NKLAKPEDMK TLRMVVSGGT TLPLKIAEDF KNNFGITLCE GYGLSETSPV
     VTMNSPATAK IGSIGPVVQG IEYKIMSGEN QEVAKGEAGE LVVKGDNVML GYWNLPEGTA
     AALQDGWFHT GDVVREDEEG FLYVVDRIKD IIISMGENVY PREIEELIYH YPGITECAVV
     GVPDKLRGNA GACFYAVGEG ETVNIRELKK YLQKNLALYK IPREFHEVEA LPRTSTGKIA
     KNRIIPGYQA SKKK
//
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