SYA_ZYMMO
ID SYA_ZYMMO Reviewed; 890 AA.
AC Q9RNN8; Q5NP91;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 112.
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=ZMO0845;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Um H.W., Kang H.S.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=19816441; DOI=10.1038/nbt1009-893;
RA Yang S., Pappas K.M., Hauser L.J., Land M.L., Chen G.L., Hurst G.B.,
RA Pan C., Kouvelis V.N., Typas M.A., Pelletier D.A., Klingeman D.M.,
RA Chang Y.J., Samatova N.F., Brown S.D.;
RT "Improved genome annotation for Zymomonas mobilis.";
RL Nat. Biotechnol. 27:893-894(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. {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; AF179611; AAD53924.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV89469.2; -; Genomic_DNA.
DR RefSeq; WP_011240713.1; NZ_CP035711.1.
DR AlphaFoldDB; Q9RNN8; -.
DR SMR; Q9RNN8; -.
DR STRING; 264203.ZMO0845; -.
DR EnsemblBacteria; AAV89469; AAV89469; ZMO0845.
DR GeneID; 58026651; -.
DR KEGG; zmo:ZMO0845; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_5; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 91428at2; -.
DR Proteomes; UP000001173; 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..890
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075258"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT CONFLICT 12..25
FT /note="LEYFEKNGHRIVPS -> SRIFRKEWPSDSTI (in Ref. 1;
FT AAD53924)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..191
FT /note="GPPGSP -> ASGLA (in Ref. 1; AAD53924)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="E -> K (in Ref. 1; AAD53924)"
FT /evidence="ECO:0000305"
FT CONFLICT 753..756
FT /note="SERA -> CQRS (in Ref. 1; AAD53924)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="Missing (in Ref. 1; AAD53924)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="L -> F (in Ref. 1; AAD53924)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="G -> C (in Ref. 1; AAD53924)"
FT /evidence="ECO:0000305"
FT CONFLICT 781..783
FT /note="EKV -> DKL (in Ref. 1; AAD53924)"
FT /evidence="ECO:0000305"
FT CONFLICT 787
FT /note="Q -> H (in Ref. 1; AAD53924)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="D -> E (in Ref. 1; AAD53924)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="R -> L (in Ref. 1; AAD53924)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="D -> G (in Ref. 1; AAD53924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 890 AA; 97115 MW; E93719541F848C43 CRC64;
MITTNEIRRS FLEYFEKNGH RIVPSAPLVP QNDPTLMFVN AGMVPFKNTF TGLESRPYKT
ATSSQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKERVIELA WGLITKEWGL
DPERLCVTVY HTDEEAFNLW RKIAGLPEDR IIKIATSDNF WSMGDTGPCG PCSEIFYDHG
PEIPGGPPGS PDEDGDRFVE IWNLVFMQYE QVNAETRLNL PRPSIDTGMG LERIASVLQG
VHDNYDTDTF KALIAASGEL THTATDGQFK ASHRVIADHL RAAGFLVADG VLPANEGRGY
VLRRIMRRAM RHAHLIGAKE PLMYRLVPAL LSEMGMAYPE LVRAKALIEE TLRLEETRFR
QTLANGLKIL EDETQHLKSG DTLPGAVAFR LYDTYGFPYD LTADALRARN LTVDQAGFDA
AMAEQRKAAR AAWKGSGEKA SDEIWFDIAD QLGGTEFTGY TAEKGSGQII ALIKDGKRVE
TAKQGDDITI ITNQTPFYGE SGGQKGDIGV ITGNNDLKMT VTDTQKPLGR IHAHIAKIEK
GEIKIGDDIQ LQVDINHRNR LRANHSATHL LHAALRDQLG QHVSQKGSMV SAERLRFDFS
HQKALSDQEL AAIEAEVNQQ ILNNSVVTTR LMTPESAVEA GAMALFGEKY GNEVRVLSMG
SCLNDQNEES SWSVELCGGT HVSALGQIGL FHIVSETAVS SGIRRIEAVT GEEARLWLVG
RDRLLRETAS ILKAVPEEVP TRTAAILDER RKSERALADA QKALALANAN GGQGGNNAAP
EKVGAYQFIG QVIEGLDPKA LRGLIDENKK IIESGVIALI TVNEGRASVA IGVSDSLKDK
ISAVDLVRKA VETLGGKGGG GRPDMAQGGG PNGNEAAQAL EAVKALLEKA
