ID A0A0N7J8L5_9BURK Unreviewed; 883 AA.
AC A0A0N7J8L5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00036};
DE EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00036};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036};
DE Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_00036};
GN Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036,
GN ECO:0000313|EMBL:ALK88528.1};
GN ORFNames=L63ED372_01318 {ECO:0000313|EMBL:ALK88528.1};
OS Limnohabitans sp. 63ED37-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK88528.1, ECO:0000313|Proteomes:UP000059510};
RN [1] {ECO:0000313|EMBL:ALK88528.1, ECO:0000313|Proteomes:UP000059510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK88528.1,
RC ECO:0000313|Proteomes:UP000059510};
RA Ahn J.-H., Kim S.B.;
RT "Limnohabitans sp. 2 strains.";
RL Submitted (JUN-2015) 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:0000256|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:0000256|HAMAP-Rule:MF_00036};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00036};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00036};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00036}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00036}.
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DR EMBL; CP011774; ALK88528.1; -; Genomic_DNA.
DR RefSeq; WP_062404555.1; NZ_CP011774.1.
DR AlphaFoldDB; A0A0N7J8L5; -.
DR STRING; 1678128.L63ED372_01318; -.
DR KEGG; lih:L63ED372_01318; -.
DR PATRIC; fig|1678128.3.peg.1304; -.
DR OrthoDB; 9803884at2; -.
DR Proteomes; UP000059510; 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 CDD; cd00673; AlaRS_core; 1.
DR Gene3D; 2.40.30.130; -; 1.
DR Gene3D; 3.10.310.40; -; 1.
DR Gene3D; 3.30.54.20; -; 1.
DR Gene3D; 6.10.250.550; -; 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 NCBIfam; TIGR00344; alaS; 1.
DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
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; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00036};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00036}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00036};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00036};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00036};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00036}; Reference proteome {ECO:0000313|Proteomes:UP000059510};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00036};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00036};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00036}.
FT DOMAIN 6..717
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT COILED 733..767
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 573
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 674
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
SQ SEQUENCE 883 AA; 95069 MW; 5671DE0E408EEE21 CRC64;
MSQPVISVAD IRKTFLDFFE SKGHTVVASS PLVPGNDPTL MFTNSGMVQF KDVFLGSDKR
SYVRAASVQA CLRAGGKHND LENVGYTARH HTFFEMLGNW SFGDYFKRES LEWAWELLTQ
VYKLPADKLY ATVYMEDDEA HGIWEGIFVK AGWTPERIKS ENRIIRIGDN KGGRYKSDNF
WMMADTGPCG PCSEIFYDHG AHIPGGPPGS PDEDGDRFIE IWNNVFMQFN MDETGAVTPL
PAPCVDTGMG LERLAAILQH VHSNYEIDIF DALIKAAARE TGCTDLNNKS LRVIADHIRA
TAFLVSDGVV PSNEGRGYVQ RRIVRRAIRH GYLLGQKTPF FHKLVPDLVK LMGAAYPNMA
DQADRIADVL RVEEERFFET LQSGMQILDA ALEGGVKVLP GEVAFKLHDT YGFPLDLSAD
VCRERGLSVD EAGFANAMEK QKAQARAAGK FKMDKALDYS GEGNDFVGYD DLTANAKVLA
LYADGNAVTE LKAGQSGVVV LDTTPFYAES GGQVGDQGMI HNAGGQFNVL DTLKIKADVF
GHHGEIKSGS LKVGDVVQAH VDMAVRAATV RNHSATHLMH KALREVLGSH VQQKGSLVNA
ERTRFDFAHN APVTDAEIRQ IEAQVNAEIL ANAAAQARVM DIESAQKTGA MMLFGEKYGE
TVRVLDIGSS RELCGGTHVK ATGDIGLFKI VGEGGVAAGV RRIEAVTGEN ALAYLQSLED
TVTQAAGSLK AQPAELNNRI AQVLDQVKAL EKELAAAKGK LASAQGDELM KQAVDVKGVK
LLVAQLEGAD AKTLRDTVDK LKDKLKTAVV LLTAVDGDKV QIAAGVTADT TGKVKAGELA
SFVAGQVGGK GGGKPDMAMA GGSTPAALPA ALASVQAWVS ERV
//
