ID A0A1U9K2M2_9BURK Unreviewed; 872 AA.
AC A0A1U9K2M2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 13-SEP-2023, entry version 24.
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 ORFNames=PAEH1_04200 {ECO:0000313|EMBL:AQS52297.1};
OS Paenalcaligenes hominis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Paenalcaligenes.
OX NCBI_TaxID=643674 {ECO:0000313|EMBL:AQS52297.1, ECO:0000313|Proteomes:UP000189369};
RN [1] {ECO:0000313|EMBL:AQS52297.1, ECO:0000313|Proteomes:UP000189369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15S00501 {ECO:0000313|EMBL:AQS52297.1,
RC ECO:0000313|Proteomes:UP000189369};
RA Mukhopadhyay R., Joaquin J., Hogue R., Kilaru A., Jospin G., Mars K.,
RA Eisen J.A., Chaturvedi V.;
RT "Complete Genome Sequence of Paenalcaligenes hominis, Isolated from a
RT paraplegic Patient with neurogenic bladder.";
RL Submitted (JAN-2017) 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; CP019697; AQS52297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9K2M2; -.
DR STRING; 643674.PAEH1_04200; -.
DR KEGG; phn:PAEH1_04200; -.
DR OrthoDB; 9803884at2; -.
DR Proteomes; UP000189369; 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:UP000189369};
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 1..705
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT COILED 721..755
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 561
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036"
SQ SEQUENCE 872 AA; 95331 MW; 268F48B43E73B3DD CRC64;
MKTSEIRQKF LSFFQERGHE IVPSSSLIPA NDPTLLFTNA GMVQFKDVFT GKETRPYTSA
TSSQRCVRAG GKHNDLENVG YTARHHTFFE MLGNFSFGDY FKEDAIRYAW ELLTKTYGLP
AEKLWVTVYH EDDEAYAIWN EQIGVPAERI IRIGDKGGRY VSDNFWQMAD TGPCGPCSEI
FYDHGPDVWG GPPGSPDEDG DRYIEVWNLV FMQFDRDAEG NLNPLPKPCV DTGMGLERIS
AVLQHVHSNY EIDLFQHLIQ AAARETHTQD LSNNSLKVIA DHIRACAFMI VDGVIPSNEG
RGYVLRRIVR RALRHGHKLG QNQAFFYRLV ADLATHMGEA YPELIQQQSR IEQILKQEEE
RFSETLEHGM KILESALANL PKDGVLDGQT LFTLYDTYGF PVDLTADICR EREVEVDLAG
FDQAMQRQRE MARASGKFKT AVADLKYDGV ETQFEGYEQL TTAATVTALY VDGSAVEQIN
EGQEAIVVLD STPFYAESGG QVGDTGVLQG ATAAFTVQDT QKLLAQVFGH HGVVTQGSLK
VGDSVQAQVD ADHRQHTIRN HSATHLMHKA LKIVLGDHVQ QRGSLVDADK TRFDFAHDSA
LSIEQIAQVE AIVNQEILAN QPVAAQLMSF DDAVSGGAMA LFGEKYGDEV RVLDIGFSRE
LCGGTHVART GDIGLFKIVS EGGVAAGVRR IEAITGENAL AWVQKREATL QGAAASLRTQ
PEKLAERLTQ LQTQLRELER ERDQLKDKLA ASAGQDLVSQ AIELAGGVKL LVADLPAADP
KSLRTTVDQL KDKLKSAVVL LATAKDDKIS LVAGVTADIN ANVKAGELIG MVAAQVGGKG
GGRPDMAMGG GSDSAALPAA LGSVQAWVES QL
//
