ID SYA_AKKM8 Reviewed; 942 AA. AC B2UKT4; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 22-FEB-2023, 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=Amuc_1383; OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC OS 81048 / CCUG 64013 / CIP 107961 / Muc). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Akkermansiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP RC 107961 / Muc; RX PubMed=21390229; DOI=10.1371/journal.pone.0016876; RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M., RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.; RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin RT degrader, and its use in exploring intestinal metagenomes."; RL PLoS ONE 6:E16876-E16876(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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001071; ACD05207.1; -; Genomic_DNA. DR RefSeq; WP_012420422.1; NC_010655.1. DR AlphaFoldDB; B2UKT4; -. DR SMR; B2UKT4; -. DR STRING; 349741.Amuc_1383; -. DR EnsemblBacteria; ACD05207; ACD05207; Amuc_1383. DR KEGG; amu:Amuc_1383; -. DR eggNOG; COG0013; Bacteria. DR HOGENOM; CLU_004485_1_1_0; -. DR OMA; YHHTMFE; -. DR OrthoDB; 9803884at2; -. DR BioCyc; AMUC349741:G1GBX-1469-MON; -. DR Proteomes; UP000001031; 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 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 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 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..942 FT /note="Alanine--tRNA ligase" FT /id="PRO_0000347482" FT BINDING 586 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036" FT BINDING 590 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036" FT BINDING 695 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036" FT BINDING 699 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036" SQ SEQUENCE 942 AA; 103645 MW; ED53F46EB999D0D9 CRC64; MMTATEIRQS FLDFFREKQH TVVPSASLMP QSPGLLFTNA GMNQFVPYFL GVWTPPWTPA RATDTQKCIR AGGKHNDLED VGYDSYHHTF FEMLGNWSFG DYFKREAIRW AWELVVERWG FPAERLYATV YAPDKSKGDP GEFDREAWDF WAELFRSRGL DPDVHIVHGN VKDNFWMMGE TGPCGPCSEL HVDLTPEGNT KGSLVNKDSD QCIEIWNLVF IQYNAESDGS MRNLPACHVD TGMGFERACS IMQCTNGFKD FSRKPSNYAT DVFRPLFDRL EVLSGRKYAD VYPAPGSKRV DAEDGTLQEA IAFRVIADHL RTLSFSIADG ILPGNNGRNY VLRRILRRAV RYGRRLGFTQ PFLAELVDTL VESFGQVFPE LAARATTVKE VLNREEASFN ETLDRGLELF DAETASAGKV SGEFAFKLYD TYGFPIDLTA LLAEERGLDI DMERFNRLME EQRERARAAR KSEVVRALDL KTDAVTEFTG YDVDECAATV LEVSRQGDSL FIITDKTPFY AEMGGQVSDA GLIEIGGESY HVMAVQQIGN ARAHVVEARP GLEVKPGDRV HLSIDAERRR RIEAHHTATH LLHCALHQVV SPDAAQQGSF VSEDRLRFDF NSSAVSPDQL RLIEEKVNGW IEESLPVHCT ERAYADVKGN AAIAQFFGDK YGDVVRVVQV GGCRDGLDGV SMEFCGGTHI ANTKNIGLFK IKSEGAIASG VRRIEAMTGD AALEMIRQHV VAKSLEIAKA VEKIKEVNYE LADMGLEQVP VPTIEGKPGL TALGASDIRT VNDSLARFDA SVEHFKQTAL DAEKKLKKAR AGQSAAKADA LLNEWLSDAP SSLIQVAEGA GELLQELLNG LKKRQYAGAA FLLCVDSSSL LLGAYCGKDA IADGLSAGDM IREVAALAGG KGGGRADQAR GSAPQDADPQ ALAAAARNII NG //