SYA_HAEDU
ID SYA_HAEDU Reviewed; 874 AA.
AC Q7VLK0; Q9F666;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=HD_1429;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-874.
RA Sun S., Gibson B.W., Campagnari A.A., Munson R.S. Jr.;
RT "Haemophilus ducreyi strain Hd9 strain produces a truncated
RT lipooligosaccharide due to a mutation in UDP-glucose pyrophosphorylase
RT (galU).";
RL Submitted (AUG-2000) 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=AAG23689.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017143; AAP96235.1; -; Genomic_DNA.
DR EMBL; AF297520; AAG23689.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_010945284.1; NC_002940.2.
DR AlphaFoldDB; Q7VLK0; -.
DR SMR; Q7VLK0; -.
DR STRING; 233412.HD_1429; -.
DR PRIDE; Q7VLK0; -.
DR EnsemblBacteria; AAP96235; AAP96235; HD_1429.
DR KEGG; hdu:HD_1429; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_6; -.
DR OMA; YHHTMFE; -.
DR Proteomes; UP000001022; 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..874
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075121"
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 874 AA; 96611 MW; B990F56DF8C59D07 CRC64;
MKTTSEIRQS FLDFFNSKGH TVVPSSALVP ENDPTLLFTN AGMNQFKDVF LGLEKRPYTR
ATTAQRCVRA GGKHNDLENV GYTARHHTFF EMMGNFSFGD YFKHDAIQFA WEFLTSEKWL
HLPKEKLYVT VYETDDEAYD IWHKTVGVPS EHIIRIGDNK GVPYASDNFW AMGDTGPCGP
CTEIFYDHGE SFWGGLPGTA EEDGDRYIEV WNIVFMQFNR QADGTLAKLP KPSVDTGMGL
ERMTAVMQHV NSNYETDIFQ TLIKEVATLL HVADLDNKSL RVIADHIRAC SYLIVDGVIP
SNEGRGYVLR RIIRRAVRHG NLLGAKEAFF YKLVPTLAKV MGQAGEILTD KQSYIQKTLK
TEEEQFARTL ERGLALLEEA LTKVENQTLS GEVAFKLYDT YGFPLDLTAD VCRERDIVID
EASFEIEMTA QRERAKSSSN FGADYNSVIK VEAETAFIGY DCFNAEAKVI ALFSNGQAVD
KVQSGESAVV VLDKTPFYAE MGGQVGDSGL ITTAFCQFAV ADTQKYGQVF GHIGQVVSGS
LAIGDIISAQ VDIARRQAIT ANHSATHLLH SALRQVLGEH VVQKGSLVSE NVLRFDFSQS
QAVSKAQLEE IERIVNRQIR QNLAVTIETM DIETAKEKGT VALFGEKYGD VVRVVGMTDF
SIELCGGTHV KHTGEIGLFK LISESAVAAG IRRVEALTAE NAINWLHNQQ KIIHQSAELL
KTDSLSLVDK IYQLQDKIKR NEKELQHFKD KLAAQAGAEL AKQVVQINGI NVVIQKLEGI
ESKSLRTMVD DLKNQLSSVI VVFGSVSADK VNLIVGVTKD LSNKVNAGEL VGLIAQQVGG
KGGGRPDMAM AGGTEPQHLD TALAFAKQWI HSKL
