SYA_CLOAB
ID SYA_CLOAB Reviewed; 881 AA.
AC Q97IG3;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=CA_C1678;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79644.1; -; Genomic_DNA.
DR PIR; A97107; A97107.
DR RefSeq; NP_348304.1; NC_003030.1.
DR RefSeq; WP_010964985.1; NC_003030.1.
DR AlphaFoldDB; Q97IG3; -.
DR SMR; Q97IG3; -.
DR STRING; 272562.CA_C1678; -.
DR EnsemblBacteria; AAK79644; AAK79644; CA_C1678.
DR GeneID; 44998173; -.
DR KEGG; cac:CA_C1678; -.
DR PATRIC; fig|272562.8.peg.1881; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_9; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 91428at2; -.
DR Proteomes; UP000000814; 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..881
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075093"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 572
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"
FT BINDING 674
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 881 AA; 99662 MW; EE5B1A69B1A47483 CRC64;
MKYMGLNDIR ESYLSFFEKK EHLRLPSFSL IPKNDKSLLL INAGMAPLKP YFTGLQTPPK
TRVTTCQKCI RTGDIENIGK TSRHGTFFEM LGNFSFGDYF KEEVISWAWE YITEVLKFPK
DRIYITIYLD DDEAFKIWTE KAGVDPSRIF RFGKEDNFWE HGSGPCGPCS EMHFDRREKP
DLIKTREKFI ELQDKDEVIE FWNLVFTQFD KDEDGNYNKL KNPNIDTGMG LERIATIMQN
TDSIFEIDTI REVLDAVCKI CNVKYGENHK NDVSLRIITD HIRSVTFMIS DGILPSNEGR
GYVLRRLLRR AARHGKTLGI EKTFLCGLCD VVIKNSKGAY KELEEKQDYI KNVIEIEEKR
FDETLDSGME ILKNYIDELS LENKKVMSGE KAFRLYDTYG FPVELTQEIL EEKGIEIDMN
DFHSEMEKQK NRARDAREES NYMGKEIKLI DKLPESVTTK FVGYNSTSTD SKVEVLIKDD
EFVSTINEGE SGIVVTEETP FYAEMGGQIG DKGIIFGKNG EAKVVDCKNN ISGKIIHIVQ
VVKGSIEKNE NVTLEVNYKK RKDICKNHTA THMLQAALKK VVGSHINQSG SYVDNERLRF
DFTHFTALTD EEILKVEAMV NDEIMAAYDV KTDIMSVDEA KKTGAMALFD EKYGNRVRVV
SVGDFSRELC GGTHVNNSGE IGLFKIISES GVAAGIRRIE AITGKEAVRY TEENDNLIRN
IEQELKCSKK DILNKINQYH SELKEKEKEI NILKGKLASG FEENILSSVK EVSGVKYVAS
EVKGISGDTL RELCDKVRNK IDDGMVLLAS KDGEKVQFVA MASKNAVKKG VHCGKVIKEV
ASMCGGNGGG RPDMAQAGGK DGEKLETALK EVGNIMEKLV K
