SYA_CHLL3
ID SYA_CHLL3 Reviewed; 887 AA.
AC Q3B1I7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=Plut_1952;
OS Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS luteolum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=319225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 273 / BCRC 81028 / 2530;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelodictyon luteolum DSM 273.";
RL Submitted (AUG-2005) 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; CP000096; ABB24794.1; -; Genomic_DNA.
DR RefSeq; WP_011358664.1; NC_007512.1.
DR AlphaFoldDB; Q3B1I7; -.
DR SMR; Q3B1I7; -.
DR STRING; 319225.Plut_1952; -.
DR EnsemblBacteria; ABB24794; ABB24794; Plut_1952.
DR KEGG; plt:Plut_1952; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_10; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 91428at2; -.
DR Proteomes; UP000002709; 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; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..887
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347717"
FT REGION 425..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 573
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"
FT BINDING 676
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 887 AA; 97912 MW; BA2F79844484D508 CRC64;
MHSREIRQSF LDFFAAKSHT IVRSAPVIPA DDPTLLFTNA GMNQFKDVFL AKGTRPYTRA
ADTQKCIRAS GKHNDLEDVG RDTYHHTFFE MLGNWSFGDY YKEEAISWAW ELLTEVWKLP
ADRLYATVYH DDDESARIWA EKTSIEPSHI LRFGDKDNFW EMGETGPCGP CSEIHIDLTP
DGSGKELVNA GDHRAIELWN LVFIQYDRQP DGRLEPLPQR HVDTGMGFER VCAVMQSKAS
NYDTDVFLPL FQRLSELTGV TYGASMDGRQ DIAMRVIADH ARTLTFALSD GAMPSNEGRG
YVLRRILRRA LRYSRDLGCS GPILHQLVGT LADSMGDVFG ELRDRRDAVE RIIRAEEESF
ITTLDRGMEI FGELAAATAR AGGRMLKGED AFKLYDTYGF PFDLTRLLAT EAGLDVDGEG
FEHCMQEQKS RARSDRREKQ QTGDGAGSWQ WFSDSHATTF LGYDRLAMPS TIIGAAHASG
HLLLVLAETP FYAESGGQTG DRGWLESAAY RMQVTDTRKD GDSFVHVVSR AFDKVRDTEI
DPMDIVIEEA TPVDASVERI LRQETERNHT ATHLLHAALR RILGSHVQQK GSFVTSERLR
FDFSHFSKMT PEEIQAVEAE VNEHIRCAAH VSKHADLPYD EAIAKGALAF FGDKYAERVR
MVEVPGISAE LCGGTHVDNI GQIGIFKIIS ESSAAAGIRR IEALTGRAAE MLLWKEYHEL
QDVRQQLKLK ADEAVAEKLA ELQEEKKELE KELAGLKSAS VIDALVRDAT SAEEIGGCRI
VTKVLEGVDA DTLRSAAMAL REKLPVSAGL LCSIADGKVS LAAFSSDVAV KEKGIDAGKL
IRLAAAAVKG GGGGRAELAT AGGKNPDGVA EACRIFAEDV RRIAGAV
