ID A0A059ZTE3_ACIBA Unreviewed; 878 AA. AC A0A059ZTE3; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JAN-2015, entry version 5. DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00015689}; DE EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00015673}; DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036}; GN Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036}; GN ORFNames=BL01_15570 {ECO:0000313|EMBL:AIA53181.1}, GQ86_11415 GN {ECO:0000313|EMBL:KFB62834.1}, IX88_07955 GN {ECO:0000313|EMBL:AIL75110.1}, LH92_05680 GN {ECO:0000313|EMBL:KGF59377.1}; OS Acinetobacter baumannii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=470 {ECO:0000313|EMBL:AIA53181.1}; RN [1] {ECO:0000313|EMBL:AIA53181.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AC29 {ECO:0000313|EMBL:AIA53181.1}; RA Lean S.S., Suhaili Z., Yeo C.C., Thong K.-L.; RT "Comparative genomics of polymyxin-resistant and susceptible RT Acinetobacter baumannii isolated from the same patient."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KFB62834.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TCM206 {ECO:0000313|EMBL:KFB62834.1}; RA Chen Y.; RT "Draft genome sequence of Acinetobacter baumannii TCM206 in China."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AIL75110.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB031 {ECO:0000313|EMBL:AIL75110.1}; RA Loewen P.C., Kumar A.; RT "Genome sequence of Acinetobacter baumannii AB031."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:KGF59377.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MAR002 {ECO:0000313|EMBL:KGF59377.1}; RA Alvarez-Fraga L., Rumbo-Feal S., Merino M., Bou G., Poza M.; RT "Complete genome of a biofilm superproducing strain of Acinetobacter RT baumannii."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a CC two-step reaction: alanine is first activated by ATP to form Ala- CC AMP and then transferred to the acceptor end of tRNA(Ala). Also CC edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its CC editing domain. {ECO:0000256|HAMAP-Rule:MF_00036, CC ECO:0000256|SAAS:SAAS00015829}. CC -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP + CC diphosphate + L-alanyl-tRNA(Ala). {ECO:0000256|HAMAP- CC Rule:MF_00036, ECO:0000256|SAAS:SAAS00015802}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00036}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00036}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|SAAS:SAAS00166766}; CC Note=Binds 1 zinc ion per subunit. CC {ECO:0000256|SAAS:SAAS00166766}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036, CC ECO:0000256|SAAS:SAAS00015710}. CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic CC domain, the editing domain and the C-terminal C-Ala domain. The CC editing domain removes incorrectly charged amino acids, while the CC C-Ala domain, along with tRNA(Ala), serves as a bridge to CC cooperatively bring together the editing and aminoacylation CC centers thus stimulating deacylation of misacylated tRNAs. CC {ECO:0000256|HAMAP-Rule:MF_00036}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000256|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; CP007535; AIA53181.1; -; Genomic_DNA. DR EMBL; CP009256; AIL75110.1; -; Genomic_DNA. DR EMBL; JMRW01000030; KFB62834.1; -; Genomic_DNA. DR EMBL; JRHB01000001; KGF59377.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1. 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. 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 TIGRFAMs; TIGR00344; alaS; 1. DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015678}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015856}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015877}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015738}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015702}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015761}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015671}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015783}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00015697}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00015895}. FT METAL 562 562 Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}. FT METAL 566 566 Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}. FT METAL 670 670 Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}. FT METAL 674 674 Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}. SQ SEQUENCE 878 AA; 96528 MW; 48DC937CBAF0C6F6 CRC64; MTSAEIREAF LRYFETQGHT RVASSSLVPA NDPTLLFTNA GMNQFKDCFL GLEKRDYVRA TTSQKCVRAG GKHNDLDNVG YTARHHTFFE MLGNFSFGDY FKRDALKFAW EFLTSEQWLA LPKDKLYVTV YHTDDEAYDI WNKEIGLAPE RIIRIGDNKG EKYASDNFWA MGDTGPCGPC SEIFFDHGEH IWGGLPGSPE EDGDRFIEIW NNVFMQFNRT ADGVLHPLPA PSVDTGMGLE RISAVLQHVN SNYDIDLFQH LLKAAANIIG IEDEGQPSLR VVADHARSCC FLIADGVNPS NEGRGYVLRR IIRRAVRHGN KLGATGTFFY KMLQPLIEVM GQAYPELEAR REVIEATLIR EEEQFAKTLE QGLKLLEGEL AQLKDKTIPG ATVFKLYDTY GFPTDLTADI ARERGFIIDE AGFEVEMAAQ RQRARDAGKF AVDYNNIVKV EGETQFDGYT NTTGQGQIVA IYKDGVQVDE VSEGDEALIV LNQTPFYAES GGQIGDTGIF KNETGIFEVQ DTKKSGGAFV HQGIVTVGNL KTSQNVEAIV KADIREATAR NHSATHLLHA ALRQILGSHV QQKGSLVASD ILRFDFANDQ PVSFEQLQQV ERLVNAEIIA NTAVTTELLD IETAKAKGAM MLFGEKYGDE VRVLSMGSVI DEKNFSIELC GGIHVKRTGD IGLFKITSEG GVAAGVRRIE AVTGTKALEV VQKADHDIQH INSLLKAQKD QTVERVQANV ELVSALQKQI EQLNQKLANF QAADLIDQVQ TIAGRQTLIT TVQGVDAKAL RNLHDSVKSK LENAVIVLAG VEGDKVSLLA SVASQYTANL KAGDIIKHLA TELGGKGGGK PDLAQGGAPL NEKFGQVMAA LPAWLEQK //