SYA1_LACP7
ID SYA1_LACP7 Reviewed; 879 AA.
AC A9KMW7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Alanine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00036};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00036};
DE AltName: Full=Alanyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00036};
DE Short=AlaRS 1 {ECO:0000255|HAMAP-Rule:MF_00036};
GN Name=alaS1 {ECO:0000255|HAMAP-Rule:MF_00036}; OrderedLocusNames=Cphy_2617;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000885; ABX42978.1; -; Genomic_DNA.
DR RefSeq; WP_012200630.1; NC_010001.1.
DR AlphaFoldDB; A9KMW7; -.
DR SMR; A9KMW7; -.
DR STRING; 357809.Cphy_2617; -.
DR EnsemblBacteria; ABX42978; ABX42978; Cphy_2617.
DR KEGG; cpy:Cphy_2617; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_9; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 91428at2; -.
DR Proteomes; UP000000370; 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..879
FT /note="Alanine--tRNA ligase 1"
FT /id="PRO_0000347571"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 570
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 668
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 879 AA; 96593 MW; 0D15710A4B7B7E7E CRC64;
MKVYGVNELR KMYLDFFESK GHLKLNSFSL VPQNDKSLLL INSGMAPLKP YFTGQEIPPK
KRVTTCQKCI RTGDIENIGK TARHGTFFEM LGNFSFGDYF KHEAIAWSWE FLTEVVGLSG
DRLYPSIYLE DDEAFDIWNK EVGIAPERIF RMGKADNFWE HGAGPCGPCS EIYYDRGEKY
GCGDPNCTVG CECDRFIEVW NNVFTQFNSD GNGNYEELEN KNIDTGMGLE RLAVVVQDVD
TLFDIDTMKA IRDHVCKMAN AEYKVDPKKD MSIRLITDHI RSVTFMTSDG IIPSNEGRGY
VLRRLLRRAA RHGRLLGIQG KFLAELSKTV IAESKDGYPE LEEKKEYILK VLTIEEEKFN
KTIDQGLSIL SEMEEALVSN GTKTLNGEDA FKLYDTYGFP LDLTKEILEE KGFSIDEEGF
KKAMQVQRET ARSARAVTNY MGADASIYDE IDPAITSNFV GYDRTSHTSK ISVLTTETDL
TDEVVGGQTA TIIVDETPFY ATMGGQTADI GFIVGKDAEF EVEDTIKLKG GRVGHLGTVT
KGSFKVGETV TLTIDTQKRQ AIGKNHSATH LLQKALRNVL GSHVEQAGSF VTSERLRFDF
THFSALTKEE IAKVEAMVNE EIAKNVPVVT DVMSVEDAKK SGAMALFGEK YGDSVRVVTM
GDFSKELCGG THVANTGSIT VFKILSEAGI AAGVRRIEAI TSNAVFEYYK SMEEELHEAA
KVAKTEPASL VKRIESLQEE LKTALSENEK LKAKLANNSL GDVMNQVVEV KGVKLLASKV
TDADMNGLRN LGDQLKEKLG ECVILLASAS EDKVNLIAMA TDGAMAKGAH AGNLIKEVAV
LVGGGGGGRP NMAQAGGKNP SGIDAAIEKA VSVVENQIK
