SYA_MYCPN
ID SYA_MYCPN Reviewed; 900 AA.
AC P75368;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
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}; OrderedLocusNames=MPN_419;
GN ORFNames=MP422;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96070.1; -; Genomic_DNA.
DR PIR; S73748; S73748.
DR RefSeq; NP_110107.1; NC_000912.1.
DR RefSeq; WP_010874775.1; NC_000912.1.
DR AlphaFoldDB; P75368; -.
DR SMR; P75368; -.
DR IntAct; P75368; 3.
DR STRING; 272634.MPN_419; -.
DR EnsemblBacteria; AAB96070; AAB96070; MPN_419.
DR KEGG; mpn:MPN_419; -.
DR PATRIC; fig|272634.6.peg.454; -.
DR HOGENOM; CLU_004485_1_1_14; -.
DR OMA; YHHTMFE; -.
DR BioCyc; MPNE272634:G1GJ3-678-MON; -.
DR Proteomes; UP000000808; 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; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
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..900
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075156"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 900 AA; 103635 MW; 59C1A9F5A0140E6E CRC64;
MKWTTDKVRQ TWLDYFTAKG HLALPSKSLI PVNDPSLLWI NSGVATLKDY FSAKKTPPSK
RLANAQICLR VNDIENVGFT SRHQTLFEML GNFSIGDYFK EEAIGFANDL LVNHYHLDPK
RFYITVYQDD ELTFNTWLKH GIPASRIIKC DRDRNFWDLG LGPCGPCTEI YYDRGERFDP
HKVGEKLFFE DIENDRYVEV WNIVFSQFNN DGNGNYSELA QKNIDTGAGI ERLVAILQDA
PTNFDTDIFL KLIGIIEQHC KHKYDTNLYF KFDQKLNEAQ SAFRIISDHF KAITFTIAEG
VLPGPNERSY IVRRLLRRAL LACKKLDLDL KFIDPMVDAI ISVYGSYYQQ LQGKNQVVQQ
AIWKEVTAFD KTINLGLMLF EKSIAHNALQ PQVAFQLYET YGFPIEMIKE LVDKRQLQVD
WKAVEQLMEQ HRLISKQNSN TLSFEKQNEH LVNFKTASEF LYEANEITAK VIGLFDEQYQ
PVQKLHNQSG YVVFDQTVLY ATSGGQRYDE GYCINHSQND QRVSFQGVFK GPNKQHFHFF
LTGSFQLGDK VILVHDGKWR QLVKNNHSLE HLLHAALQNE IDPLIKQDGA FKSAQKATID
FNFSRALTWA ELERVEHRIR QIIQQDIQRE EIFTDLEGSQ KLNAIAYFEE EYSNHELLRV
IRFGDFSVEL CGGTHVEHTG LIENCFITDY YARGTGRWRI EIISSNETIA AYLNEQNGKL
SETINSLHNT LNNIANPALN KQKTALTKQL NHFHLPQVIT DLRKCQALLN ELKITVNELK
TEDFKWKQKQ LAEKIKQELL ELAKQDKAYV LASFAAVDPK LLSQVAQAVL NQHKNKLFVL
LNQFNNSPSF MLLGQDVSKC IQLLKAHFEL KGGGSNNFFR GSFNESVDVS KLQAILDTLQ
