SYA_BRADU
ID SYA_BRADU Reviewed; 892 AA.
AC Q89I89;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 101.
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=bll5750;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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=BAC51015.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000040; BAC51015.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_772390.1; NC_004463.1.
DR RefSeq; WP_038967195.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89I89; -.
DR SMR; Q89I89; -.
DR STRING; 224911.27354027; -.
DR EnsemblBacteria; BAC51015; BAC51015; BAC51015.
DR GeneID; 64025519; -.
DR KEGG; bja:bll5750; -.
DR PATRIC; fig|224911.44.peg.5683; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_5; -.
DR InParanoid; Q89I89; -.
DR OMA; YHHTMFE; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
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..892
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075074"
FT REGION 857..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 682
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 892 AA; 96773 MW; 2298D4ED467C149A CRC64;
MSGVNEIRST FLNFFAENGH EIVPSSPLVP RNDPTLMFTN AGMVQFKNVF TGVEKRPYQR
ATTSQKCVRA GGKHNDLDNV GYTARHLTFF EMLGNFSFGD YFKERAIELA WKLITKDFGL
NKDKLLVTVY HTDDEAHGLW KKIAGFSDDR IIRIPTSDNF WAMGDTGPCG PCSEIFIDRG
DHIWGGPPGS PEEDGDRFLE FWNLVFMQYE QVTKEERVDL PRPSIDTGMG LERMACIMQG
VDSVFETDLF RHLIDATASA LGSGPNEQTV ASFRVIADHL RSSAFLVSDG VLPSNEGRGY
VLRRIMRRAM RHAQLLGAKE PLMHRLVWAL VREMGQAYPE LMRAEKLIEE TLRLEETRFR
KTLTRGLAIL DEKSASLKKG DMFDGDVAFT LYDTYGFPLD LTQDALKSRG IGVDQSAFTD
AMERQKAKAR ESWKGSGEAA SEAIWFPLRE KLGATEFLGY ETESAEGVVS ALVKDGQEAA
SLKAGETGAL VLNQTPFYAE SGGQVGDTGV LLGEGGVKFR VTDTQKKLGD LFVHVGTVES
GELKLGTALQ LEVDHSRRSS IRAHHSATHL IHEALRQVLG DHIAQRGSMV APDRLRFDFV
HPKPITAEEL ARVEDIANDV VLENDEVTTR VMGVDEAREA GARALFGEKY GDEVRVVSMG
RTARERGANA LGWSVELCGG THVRRTGDIG LITLTGESAV ASGVRRIEAL TGNYARKHAN
DTMALAKTAA NELRTSIDDV PARITALMEE RKKLERELSD ARKKLAMGGG AAASNGAASG
VREVGDVKLM ARAVEGIEMK DLKSLADDGK KQIGSGVVAI VGVTGDGKAG IVVGVTADLT
ARFNAVNLVR VASEALGGKG GGGRPDMAQA GGPDGAKAPE ALAAIEKAMA GA
