SYA_PELTS
ID SYA_PELTS Reviewed; 877 AA.
AC A5D3F4; A5D3F5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00036};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00036};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_00036};
GN Name=alaS {ECO:0000255|HAMAP-Rule:MF_00036};
GN OrderedLocusNames=PTH_1060/PTH_1061;
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI;
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC domain. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00036};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00036};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00036};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00036}.
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00036}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF59241.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAF59242.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AP009389; BAF59241.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AP009389; BAF59242.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; A5D3F4; -.
DR SMR; A5D3F4; -.
DR STRING; 370438.PTH_1060; -.
DR EnsemblBacteria; BAF59241; BAF59241; PTH_1060.
DR EnsemblBacteria; BAF59242; BAF59242; PTH_1061.
DR KEGG; pth:PTH_1060; -.
DR KEGG; pth:PTH_1061; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_0_3_9; -.
DR Proteomes; UP000006556; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF101353; SSF101353; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..877
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347718"
FT BINDING 564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 670
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 877 AA; 96721 MW; 0B221E8B91CC0B93 CRC64;
MTGNEIRESY LKFFEKKGHK ILPSASLIPL NDPSILWTAA GMVPFKPFFT GAAKPEYTRV
TTCQKCIRTP DIESVGKTAR HHTFFEMLGN FSFGDYFKES AIPWAWEFVT EHLRLPADKL
WISIFLDDDE AFEIWNKTVG VPAGRIVRMG KDTNFWEIGV GPCGPCSEIY VDLGAERGCG
SPECKVGCDC DRFLEIWNLV FIQFFKDEEG NYTPLTSKGI DTGFGLERVA SVMQGVPTNF
DTDLFREIMD FTAGLFGLKY GVDGRVDVAL KVIADHCRAI TFAVADGALP SNEGRGYVIR
RLLRRAVRFG RLLGIEDPFL HEVSGAVVRQ MGRVYPELVT QREHVFRVIR REEERFGETL
AQGTEMLNRL IAEARQAGSA VVSGEDAFRL YDTYGFPLEL TQEMAGEQGL TVDTDGFGRA
MEEQRQRARS ARQETDYISG RDAMFKKMRE EVGETVFVGY DALEATGRVL RIVQGGKRLE
SAQAGEEVEF ILDVTPFYAE SGGQVSDRGK VTAADLEVEI HEVTKPVENL FVHRGKVVAG
ILKEHDTVTA RVDPARRAAT CRNHSATHLL HKALKEVLGG HVNQAGSLVE PERLRFDFTH
YAAATPEELQ KVEELVNRMV LSALPVEAFE TSLAEARKMG AAALFGEKYG ERVRVVKMGD
FSLELCGGTH LRNTAEVGLF KLLGESSVGA GLRRIEAVTG EGALSYVKAK EEQLAEIARL
VKAAPHEAVR RVEGLLQTVR DLEAENEALQ ARLARYQVQD LMDRLREVKG VKVLAGQAAA
PDMDSLRGMV DLLRDRVGSG VIVLGSAGEN RVNLVAAVTK DLVEKGLHAG KLVKELAPVV
GGGGGGRPEM AQAGGKDPSR LKEALEKTYK AVESQLK
