SYA_ARCFU
ID SYA_ARCFU Reviewed; 906 AA.
AC O28029;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=AF_2255;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP MUTAGENESIS OF CYS-703.
RX PubMed=17327676; DOI=10.1107/s090744490605640x;
RA Fukunaga R., Yokoyama S.;
RT "Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii.";
RL Acta Crystallogr. D 63:390-400(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-739 WITH AN ALANYL-ADENYLATE
RP ANALOG, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 737-906, FUNCTION,
RP ZINC-BINDING, COFACTOR, SUBUNIT, AND DOMAIN.
RX PubMed=19423669; DOI=10.1073/pnas.0901572106;
RA Naganuma M., Sekine S., Fukunaga R., Yokoyama S.;
RT "Unique protein architecture of alanyl-tRNA synthetase for aminoacylation,
RT editing, and dimerization.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8489-8494(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). Incorrectly charged
CC aminoacyl-tRNA(Ala) is also edited in situ by the editing domain.
CC {ECO:0000269|PubMed:19423669}.
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;
CC Evidence={ECO:0000269|PubMed:19423669};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19423669};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19423669}.
CC -!- INTERACTION:
CC O28029; O28029: alaS; NbExp=3; IntAct=EBI-15779415, EBI-15779415;
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. {ECO:0000269|PubMed:19423669}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE000782; AAB89002.1; -; Genomic_DNA.
DR PIR; G69531; G69531.
DR RefSeq; WP_010879744.1; NC_000917.1.
DR PDB; 2ZTG; X-ray; 2.20 A; A=1-739.
DR PDB; 2ZVF; X-ray; 3.20 A; A/B/C/D/E/F/G/H=737-906.
DR PDB; 3WQY; X-ray; 3.30 A; A/B=1-906.
DR PDB; 3WQZ; X-ray; 3.49 A; A/B=1-906.
DR PDBsum; 2ZTG; -.
DR PDBsum; 2ZVF; -.
DR PDBsum; 3WQY; -.
DR PDBsum; 3WQZ; -.
DR AlphaFoldDB; O28029; -.
DR SMR; O28029; -.
DR DIP; DIP-48856N; -.
DR STRING; 224325.AF_2255; -.
DR PRIDE; O28029; -.
DR EnsemblBacteria; AAB89002; AAB89002; AF_2255.
DR GeneID; 24796018; -.
DR KEGG; afu:AF_2255; -.
DR eggNOG; arCOG01255; Archaea.
DR HOGENOM; CLU_004485_4_0_2; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 7896at2157; -.
DR PhylomeDB; O28029; -.
DR BRENDA; 6.1.1.7; 414.
DR EvolutionaryTrace; O28029; -.
DR Proteomes; UP000002199; 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:0002161; F:aminoacyl-tRNA editing activity; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IMP:UniProtKB.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_A; Ala_tRNA_synth_A; 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; IPR022429; Ala-tRNA_lgiase_arc.
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; TIGR03683; A-tRNA_syn_arch; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..906
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075260"
FT BINDING 600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 703
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 707
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MUTAGEN 703
FT /note="C->A: Loss of tRNA editing activity."
FT /evidence="ECO:0000269|PubMed:17327676"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:2ZTG"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3WQZ"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:2ZTG"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:2ZTG"
FT TURN 105..110
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 116..127
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:2ZTG"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 143..155
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 196..205
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 208..220
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 231..246
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 266..274
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:3WQY"
FT HELIX 285..301
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 307..320
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 324..352
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 361..379
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 386..397
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 405..437
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 442..452
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 476..482
FT /evidence="ECO:0007829|PDB:2ZTG"
FT TURN 508..510
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 516..525
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 528..534
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 555..559
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 590..614
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 620..622
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 631..635
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 642..657
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 661..668
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 669..676
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 678..681
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 688..696
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 699..702
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 711..714
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 717..726
FT /evidence="ECO:0007829|PDB:2ZTG"
FT STRAND 729..737
FT /evidence="ECO:0007829|PDB:2ZTG"
FT HELIX 738..740
FT /evidence="ECO:0007829|PDB:2ZVF"
FT HELIX 742..756
FT /evidence="ECO:0007829|PDB:2ZVF"
FT TURN 757..759
FT /evidence="ECO:0007829|PDB:2ZVF"
FT HELIX 762..764
FT /evidence="ECO:0007829|PDB:3WQY"
FT HELIX 765..799
FT /evidence="ECO:0007829|PDB:2ZVF"
FT STRAND 803..807
FT /evidence="ECO:0007829|PDB:2ZVF"
FT STRAND 809..814
FT /evidence="ECO:0007829|PDB:2ZVF"
FT HELIX 819..831
FT /evidence="ECO:0007829|PDB:2ZVF"
FT STRAND 834..841
FT /evidence="ECO:0007829|PDB:2ZVF"
FT STRAND 843..856
FT /evidence="ECO:0007829|PDB:2ZVF"
FT HELIX 858..869
FT /evidence="ECO:0007829|PDB:2ZVF"
FT STRAND 871..875
FT /evidence="ECO:0007829|PDB:3WQY"
FT STRAND 877..886
FT /evidence="ECO:0007829|PDB:2ZVF"
FT HELIX 890..904
FT /evidence="ECO:0007829|PDB:2ZVF"
SQ SEQUENCE 906 AA; 102536 MW; 2AD39B7B65C72C8B CRC64;
MTLDEEYLDI TFLTENGFVR KRCPKCGKHF WTADPEREIC GDPPCESYSF IGNPVFKKPF
ELDEMREYYL NFFERRGHGR IERYPVVARW RTDIYLTIAS IADFQPFVTS GVAPPPANPL
TISQPCIRLD DLDSVGRTGR HLTLFEMMAH HAFNYPGKEI YWKNETVAYC TELLNELGVK
KEDIVYKEEP WAGGGNAGPC LEAIVGGLEV ATLVFMNLEE HPEGDIEIKG ARYRKMDNYI
VDTGYGLERF VWASKGTPTV YDAIFPEVVD TIIDNSNVSF NREDERVRRI VAESSKLAGI
MGELRGERLN QLRKSVADTV GVSVEELEGI VVPLEKVYSL ADHTRCILFM LGDGLVPSNA
GAGYLARLMI RRSLRLAEEL ELGLDLYDLV EMHKKILGFE FDVPLSTVQE ILELEKERYR
TTVSKGTRLV ERLVERKKKL EKDDLIELYD SHGIPVELAV GIAAEKGAEV EMPKDIYAEL
AKRHSKAEKV QEKKITLQNE YPATEKLYYD DPTLLEFEAE VIGVEGDFVI LNRSAFYPES
GGQDNDVGYL IANGGKFEVV DVLEADGVVL HVVKGAKPEV GTKVKGVIDS DVRWRHMRHH
SATHVLLYSL QKVLGNHVWQ AGARKEFSKA RLDVTHFRRP SEEEIKEIEM LANREILANK
PIKWEWMDRI EAERKFGFRL YQGGVPPGRK IRVVQVGDDV QACGGTHCRS TGEIGMLKIL
KVESIQDGVI RFEFAAGEAA IEAVEEMERL LREASSILRV EPAKLPKTVE RFFEEWKDQR
KEIERLKSVI ADLWADILME RAEEFDSMKV VAEVVDADMQ ALQKLAERLA EKGAVGCLMA
KGEGKVFVVT FSGQKYDARE LLREIGRVAK GSGGGRKDVA QGAVQQLLDR EEMLDVIFRF
LSEHEG
