ID   SYA_KORVE               Reviewed;        1098 AA.
AC   Q1IJG7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Alanine--tRNA ligase;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanyl-tRNA synthetase;
DE            Short=AlaRS;
GN   Name=alaS; OrderedLocusNames=Acid345_3983;
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC   Candidatus Koribacter.
OX   NCBI_TaxID=204669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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 (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000360; ABF42983.1; -; Genomic_DNA.
DR   RefSeq; WP_011524782.1; NC_008009.1.
DR   AlphaFoldDB; Q1IJG7; -.
DR   SMR; Q1IJG7; -.
DR   STRING; 204669.Acid345_3983; -.
DR   PRIDE; Q1IJG7; -.
DR   EnsemblBacteria; ABF42983; ABF42983; Acid345_3983.
DR   KEGG; aba:Acid345_3983; -.
DR   eggNOG; COG0013; Bacteria.
DR   HOGENOM; CLU_004485_1_1_0; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 91428at2; -.
DR   Proteomes; UP000002432; 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; 2.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR00980; TRNASYNTHALA.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF101353; SSF101353; 2.
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..1098
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000347469"
FT   BINDING         779
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         783
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         883
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         887
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1098 AA;  120722 MW;  AD8FFAAA5C9A1D5A CRC64;
     MTGRCLIKYS FTPMMTGSQV RRRFLDFFIS KGHKEVHSSS LVPANDPTLL FTNAGMNQFK
     DVFLGVEKRD YNRATTSQKC VRAGGKHNDL ENVGFTNRHH TFFEMLGNFS FGDYFKKDAI
     AYAWELVTSP DWYGMQQDKL YATIFKGENG VPRDDEAYQL WLDVGVPKER VFEMGMKDNF
     WAMGDTGPCG PCSELHYDMG VASSDKKNPE CAAGECKFPC ECGRYVEIWN LVFMQFDRDA
     SGTLNPLPKP SIDTGAGLER VTAVMQGVVS NYDTDLFTPL IKRAAELTDV DEKREEAKES
     QSKSAASLRV IADHSRAATF LISDGVIPAN EGRGYVLRKI IRRGIRHGRL LGQNKPFLHD
     MVYAVRDLMQ DAYPELKETA DRVAKTVLAE ETRFANTLDI GLKKLDEDLA SLAETTRELG
     RLSWEEPKPV EFALKEVARH VFVVAQMLSP GMTFDTPGHG FLLRRGIYRA WMDLKAVGLD
     RVVRLSEIAE ALSEGETGRV QSVAKNLAHT KQILDAEQER LQSASSQLEF ELDAMEAEKK
     LAENPEMLAE QVREVFGPAL EEKVINELRG KLQSRPVYSG DKAFKLYDTF GLPLDFMVDA
     ARDQGIEFDQ AGFDAAMESQ RETARASWKG GSKLSASPIY RELAEELGTK PYPGQLAGGH
     PMITPQSIFV GYTSTEFKGA TVLAIISNGA SVAQLAPGDV AEMVLDYTPF YSESGGQIGD
     TGWLYDSTGN TVVAEVETVQ SPVQGVRAHK VTARQNIAVG DKLNAVVNAD VRRATMRNHT
     GTHLLHAALR EVLGKHVKQA GSLVDPAKLR FDFSHFTGVA DEELQDIEDI VNKEVLKNDR
     VEVIENVPID VAVNEYKAMA LFGEKYGDRV RVIKIGDFST ELCGGTHTLA TGEIGLIKVL
     HEGSVSSGVR RLEAVTGENS VRHFRKDHEL EGVVSTIVRP SEGLSPAQAL KFELDRREEE
     IKKLRKELEQ SRMKSASSAV SSATESAREV KGIKVLATRA DNIDRNQMRT LIDNLRSKLG
     SGVIVLGSVQ DGKVALIVGV TKDLTSKIQA GKIIAQVAKH VGGSGGGRPD MAEAGGKDPA
     ALDGALNATY GIVDSLLS