SYA_CHLPM
ID SYA_CHLPM Reviewed; 885 AA.
AC A4SGJ6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 80.
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=Cvib_1595;
OS Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS vibrioformis (strain DSM 265)).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 265 / 1930;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J.,
RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA Schuster S.C., Bryant D.A., Richardson P.;
RT "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL Submitted (MAR-2007) 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=ABP37605.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000607; ABP37605.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041469905.1; NC_009337.1.
DR AlphaFoldDB; A4SGJ6; -.
DR SMR; A4SGJ6; -.
DR STRING; 290318.Cvib_1595; -.
DR EnsemblBacteria; ABP37605; ABP37605; Cvib_1595.
DR KEGG; pvi:Cvib_1595; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_10; -.
DR OrthoDB; 91428at2; -.
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..885
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347732"
FT REGION 426..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 671
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"
SQ SEQUENCE 885 AA; 98142 MW; C5DB3803DC3E844F CRC64;
MKSSDIRQSF LDFFVGKSHA IVRSAPVIPA DDPTLLFTNA GMNQFKDVFL AKGTRSYSRA
ADTQKCIRAS GKHNDLEDVG RDTYHHTFFE MLGNWSFGDY YKEEAITWAW ELLTVVWKLP
EERLYATVYH DDDESFRIWE EKTSIRPDHI LRFGDKDNFW EMGETGPCGP CSEIHIDLTP
DGSGRALVNA DDPQAIELWN LVFIQYDRQV DGRLEPLPQR HVDTGMGFER VCAVMQGKSS
NYDTDVFRPL FDTITELTGV EYGASMHDPQ DIAMRVIADH ARTLSFALSD GAMPSNEGRG
YVLRRILRRA LRYAKDLGYN KPILHRLVAT VADSMGDVFP ELRDRQDAVA RIVKAEEESF
LVTLDRGIEI FNGLVGKVRG EGSSTLEGED AFKLYDTYGF PFDLTRLMAS SAGLQVDGEG
FERCMQEQKT RARQDRREKQ RGGAEEGSWE WFSDLHATEF TGYDGLEADA SIIGISRSKK
NLLLVLDRTP FYAESGGQTG DRGWIETGEY RLEVTDTQKD GDSFVHVVTR AFDNVRDSEA
DPADIAVGPG RVHASVDRKL RQATERNHTA THLLHAVLRH TLGAHVQQKG SLVNPERLRF
DFSHFSKLTP EEIDAVESAV NDCIRQAEAT LKHADVPYDD AITKGALAFF GDKYADLVRV
VEIPGISVEL CGGTHVDNVG QIGLFKIVGE SSVAAGVRRI EALTGRAAEE LMWNEYRELH
DVRQLLKMKA EEPPAEKVAA ILEERRALEK QLAELKAEVL LVKLQGDASA LEDVCGCRIV
ARVVDGADAE GLRYAAQMLR QQFPLSAGLL CSSAEGKVSL AAFASDRAVK ELGIDAGKLI
RQAAAAVKGG GGGKAEFATA GGKNPEGMED ACRVFREAVR CIVKA
