SYA_PARL1
ID SYA_PARL1 Reviewed; 892 AA.
AC A7HWA5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 76.
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=Plav_2579;
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
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=ABS64188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000774; ABS64188.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041536007.1; NC_009719.1.
DR AlphaFoldDB; A7HWA5; -.
DR SMR; A7HWA5; -.
DR STRING; 402881.Plav_2579; -.
DR PRIDE; A7HWA5; -.
DR EnsemblBacteria; ABS64188; ABS64188; Plav_2579.
DR KEGG; pla:Plav_2579; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_5; -.
DR OrthoDB; 91428at2; -.
DR Proteomes; UP000006377; 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..892
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347713"
FT REGION 852..871
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 675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 679
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 892 AA; 96512 MW; 307ED2758C62B432 CRC64;
MAGVNEIRSK YLEFFRAQGH EVVASGPLVP NNDPTLLFTN AGMVPFKNVF TGQETRPYKR
AASSQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YYKAEAIEFA WDLITKELAL
PESRLMVTIY EDDDEAHGLW KKITGLSDDK IVRLGAKSNF WQMGDTGPCG PNSEIFYDHG
DKIPGGPPGS PDEDGDRFIE IWNLVFMQYE QHEDGSRTRL PKPSIDTGMG LERIAAVLQG
THDNYSTDLM RSLIVASAEA SKSDPDGPHA VSHRVIADHL RSSSFLLADG VMPSNEGRGY
VLRRIMRRAM RHAQLVGVAE PLMWRLVPAL VRQMGDAYPE LRRAEALVTE TLRLEETRFR
ETLTRGLKLL DEEIESLGGK GVLAGEVAFK LYDTYGFPLD LTQDALRSRG MSVDQTGFDE
AMAKQRQDAR AAWSGSGEKA TEAVWFELRD KVGATEFLGY ESEIAEGKVV ALLVDGQPVD
KVEAGTDAAL ITNQTPFYAE SGGQVGDTGI VFSADGAEFP VIDTMKKLGA LHVHIGKLAR
GTLKLGDIVE MKVDKSLRDA TRANHSATHL LHEALRRVLG DHVTQKGSMV GPERLRFDFS
HPKPMTPEEI SEVETIVNRV IRQNAEVTTR LMTPEDAIAA GALALFGEKY GEEVRVLAMG
LDDENPNGTY SVELCGGTHV RRVGDIAIFK IVSESAVASG IRRIEALTGE GARAYLVAQD
RIAKEAASAL RISTEDLPAR VVSLMEERKR LERELAQAKK QLAMSGGGGS GGQESPVQEF
GGVKLIARKL EGVNPKDLRG LIDESKKQLG SGVVVLVAIS EDGKGAIAVG VTDDLTSRYN
AVELVKAGAA AMGGKGGGGR PDMAQAGGPE AEKADAALDA VKAAVGELAG AA
