ID   SYA_NITWN               Reviewed;         891 AA.
AC   Q3ST43;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=Nwi_1287;
OS   Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS   NCIMB 11846 / Nb-255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX   PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA   Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA   Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA   Hickey W.J.;
RT   "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT   Nitrobacter winogradskyi Nb-255.";
RL   Appl. Environ. Microbiol. 72:2050-2063(2006).
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}.
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DR   EMBL; CP000115; ABA04548.1; -; Genomic_DNA.
DR   RefSeq; WP_011314574.1; NC_007406.1.
DR   AlphaFoldDB; Q3ST43; -.
DR   SMR; Q3ST43; -.
DR   STRING; 323098.Nwi_1287; -.
DR   EnsemblBacteria; ABA04548; ABA04548; Nwi_1287.
DR   KEGG; nwi:Nwi_1287; -.
DR   eggNOG; COG0013; Bacteria.
DR   HOGENOM; CLU_004485_1_1_5; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 91428at2; -.
DR   Proteomes; UP000002531; 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   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; Reference proteome; RNA-binding;
KW   tRNA-binding; Zinc.
FT   CHAIN           1..891
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000347699"
FT   BINDING         564
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         568
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         678
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         682
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   891 AA;  95706 MW;  F4E49910A5ED5A38 CRC64;
     MSGVNDIRSA FLNYFAANGH QIVPSSPLVP RNDPTLMFTN AGMVQFKNVF TGVEKRPYQR
     ATTSQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKDRAIELA WKLVTQEFGL
     PKDRLTATVY IDDDGAFDLW KKIAGLPESR IIRIAGSDNF WQMGDTGPCG PCSEIFYDHG
     DRIPGGPPGS PEQDGDRFVE IWNLVFMQYE KLPDGSRPNL PKPSIDTGAG LERVAAVLQG
     KHDNYDIDLF VALIRAAADL TGADPQGPMK ASLRVIADHL RASSFLIADG VLPSNEGRGY
     VLRRIMRRAM RHAQLLGARE PLMWRLVGVL VREMGEAFPE LQRARPLIEE TLRLEETRFR
     KTLERGLSIL DEKSASLKQG DMFDGETAFT LYDTYGFPLD LTQDALRARG IGVDLASFTD
     AMEQQKAKAR ASWSGSGEAA AESIWFPLRE KLGATEFLGY ETEAAEGVVA ALVKDGEEAD
     TLKAGESGAI VLNQTPFYGE SGGQVGDTGF LIADGVRFRV TDTQKKAGDL FVHLGTVEQG
     VLAPGMALAL EVDHDRRSAI RANHSATHLL HEALRQVLGD HIAQRGSLVA PERLRFDFAH
     NKPISADELR CIEDIANDVV LENGEVTTRL MAVDDAREAG ARALFGEKYG DEVRVVSMGG
     TDRHGAASNA LGWSVELCGG THVKRTGDIG LISVVGESAV ASGVRRIEAL TGHQARHHAN
     HAIQLAKTAA GELRTSLDDM PARIASLMEE RKKLERELSE ARKKLAMGGA ASASSGATTG
     VRDVGGIKLM ARSVEGIEIK DLKSLADQGK KQLGSGVVAL VATSGDGKAS VVVGVTPDLV
     TRFSAVDLVR KASEVLGGKG GGGKPDMAQA GGPDGAKAGA ALDAIAAAMG A