SYA_VIBCH
ID SYA_VIBCH Reviewed; 860 AA.
AC Q56648; Q9KUH6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 131.
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=VC_0545;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-452.
RC STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RA Gupta N., Bhasin N., Ghosh A.;
RL Submitted (AUG-1996) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA99922.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF93713.1; -; Genomic_DNA.
DR EMBL; L78074; AAA99922.1; ALT_FRAME; Genomic_DNA.
DR PIR; G82310; G82310.
DR RefSeq; NP_230196.1; NC_002505.1.
DR RefSeq; WP_000481017.1; NZ_LT906614.1.
DR AlphaFoldDB; Q56648; -.
DR SMR; Q56648; -.
DR STRING; 243277.VC_0545; -.
DR PRIDE; Q56648; -.
DR DNASU; 2615214; -.
DR EnsemblBacteria; AAF93713; AAF93713; VC_0545.
DR KEGG; vch:VC_0545; -.
DR PATRIC; fig|243277.26.peg.521; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_6; -.
DR OMA; YHHTMFE; -.
DR BioCyc; VCHO:VC0545-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
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..860
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075241"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 665
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 860 AA; 93827 MW; 0A0EA97910F48FDB CRC64;
MFMSTDEVRR AFLSFFESKG HQIVESSSLV PANDPTLLFT NAGMNQFKDC FLGLEKRAYT
RATTAQRCVR AGGKHNDLEN VGFTARHHTF FEMLGNFSFG DYFKEDAIQY AWEFLTDVLQ
LPKERLLVTV YETDDEAFDI WNKKVGIPAD RIIRIGDKKG GKKFDSDNFW QMGDTGPCGP
CTEIFYDHGD HIWGGPPGSP EEDGDRFIEI WNNVFMQFNR HADGTMEPLP KPSVDTGMGI
ERISAIMQGV HSNYEIDVFQ TLIKAAADAI GYQDLTNQSL RVVADHIRSC AFLIVDGVMP
SNEGRGYVLR RIIRRAVRHG NKLGAQGAFF HKLVGPLAEV MGTAGVELKK QQALVEKVLR
IEEENFGRTL DRGMSILNDA LDQLSGQVLD GETVFKLYDT YGFPADLTND VARERGFSID
EAGFEQAMEE QRQRAREAGQ FGTDYNSLIK SATNTEFCGY TASRGQSVVR EMFVEGAEVS
TLSAGDKAII VLDNTPFYAE SGGQCGDTGV LKTDAGIFHV EDTQKLGNAI AHHGVIAQGV
LATGDQVDAI VDEKRRAAIS LNHSATHLLH AALRKVLGEH VAQKGSLVRA ETLRFDFSHL
EAMTAAEIKE VERLVNQEVR RNHSIETNIM NIDEAKAKGA MALFGEKYDD QVRVLSMGDF
STELCGGIHA SNTGDIGLFK IISEGGIAAG IRRIEAVTGE GALDYLDAQQ AQHDAKVSEM
AAKAKLLEKE IQQLKDKLAA KESAGLINQV KQIAGVNVLV AQLNGADNKA LRGMVDDLKN
QLSSGIIMLG NVAEGKVGLI AGVTNDLTNK VKAGELVNMV ALQVGGKGGG RPDMAQAGGT
DAHALPSALE SVDAWIAERL
