ID A0A087SIG7_AUXPR Unreviewed; 1317 AA.
AC A0A087SIG7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
GN ORFNames=F751_0548 {ECO:0000313|EMBL:KFM25521.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM25521.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM25521.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM25521.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001372};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406}.
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DR EMBL; KL662119; KFM25521.1; -; Genomic_DNA.
DR RefSeq; XP_011398417.1; XM_011400115.1.
DR STRING; 3075.A0A087SIG7; -.
DR GeneID; 23611939; -.
DR KEGG; apro:F751_0548; -.
DR eggNOG; KOG0435; Eukaryota.
DR eggNOG; KOG0657; Eukaryota.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
DR NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KFM25521.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924}.
FT DOMAIN 983..1131
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT REGION 51..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1317 AA; 143052 MW; 7A7D0EA7D994CA81 CRC64;
MPALHASGPL LGAAGPRSGT VRCALRCART ALTPWAGVAR APFSPRVPCT PLRSASTATT
QPETETGPVP ESGTGPATRH AAYPFAELEP KWQRYWEENQ TFRTPEFKDL DTSKPKFYVL
DMFPYPSGSG LHVGHPEGYT ATDILARYKR MRGFNVLHPM GWDAFGLPAE QYAIQTGTHP
AATTATNITR FRQQLRALGF SYDWRREVST ADPAYYRWTQ WVFLQLHAAG LAYQAEVPVN
WCPALGTVLA NEEVVDGLSE RGGHPVMRMP LRQWMLRITA YADRLLADLP TLDWDPAILD
QQRNWIGRSE GAAISFPLTQ RPDASGASAS PPPYPEAIEV YTTRPDTLFG ATFLVLAPEH
PATLAVATPD RAAEVQAYVA AATAKSDRQR AASGVTGVFT GAYALLPATR EPLPIWTAEY
VLGAYGTGAI MAVPAHDERD AAFAAQYRLP SRAVVRDGEA GGTVACASAA PGLTLDGLGR
AEASRAVIDW LEARGAGRGR TQYKLRDWLF ARQRYWGEPF PVVFPLGPDG SPDQTSVAIP
ESELPLVLPE VEDFTPTGTA DPPLAKATAW MQTVVPGTES PAIREASTMP QWAGSCWYYL
RYIDPDNSSR LVSKEAEAYW MPVDLYVGGA EHAVLHLLYA RFWHKVLFDL GHVSTPEPFQ
RLVSQGMILG EVEYTVHRGP GGEPVREGDA GAAAVRVRPE EVEPWAASPT GYRLRADPST
PVSARAHKMS KSRGNVINPD DVVAGYGADS LRLYEMFMGP LRDTKVWSTK GVEGVHRFLA
RVWRLGTERL AQPGVAPTPA QAAVMNRTVG RITEDTEAMR FNTAIAAMME AVNAAYKWDA
CPRPLFETLV LLLAPYAPHI AEELWQRLGH EGSLAYASWP AFDPSLVQVD SLKLPVQVNG
RVRAVIEVER EIGQGAALEA ARANEAVSRH LAGKQVVKVV WVPGRALNLI VKASRLPVVT
RAVVAERDPP AVNETSSKSS DKTRVGINGF GRIGRLTLRA AMQNPEVEIV AINDPFVNPE
YMAYMLKYDT VHGRFKGDID YDGSSLYLNG KQLAVSACMD PSEIAWGKSG ADYICEATGV
FTDTAKASAH FRGGARKVVI SAPSKDAPMF VMGVNHHEYE ACQDVVSNAS CTTNCLAPLA
KVVNDKWGIR EGLMTTVHAT TATQKTVDGP SRKDWRGGRG AAFNIIPSST GAAKAVGKVL
PALNGKLTGM AFRVPTADVS VVDLTVNLER GAEYGEIMAE LRRASQAELA GILGFTEEAV
VSSDFISDAR SSIVDASAGI QLSPTFVKLL AWYDNEWGYS NRVVDLIRHM AAVDARV
//
