SYA_SYNP6
ID SYA_SYNP6 Reviewed; 876 AA.
AC Q5N4B5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 91.
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=syc0664_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD78854.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP008231; BAD78854.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041676939.1; NC_006576.1.
DR AlphaFoldDB; Q5N4B5; -.
DR SMR; Q5N4B5; -.
DR STRING; 269084.syc0664_c; -.
DR EnsemblBacteria; BAD78854; BAD78854; syc0664_c.
DR KEGG; syc:syc0664_c; -.
DR eggNOG; COG0013; Bacteria.
DR Proteomes; UP000001175; 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; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..876
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075227"
FT BINDING 560
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 876 AA; 94671 MW; 1F5340667A9C0E03 CRC64;
MAAPALSGDQ IRETFLKFFE GKGHRRLPSA SLIPEDPTVL LTIAGMLPFK PIFLGQQVAE
VPRATTSQKC IRTNDIENVG RTARHHTFFE MLGNFSFGDY FKKEAIAFAW ELVTEVFQVP
AERLAVSVFE EDDEAFAIWR DQIGVPEARI QRLGAKDNFW ASGPTGPCGP CSEIYYDFHP
ELGNDGLDLE DDSRFIEVYN LVFMQYNRDA AGNLTALEKQ NIDTGMGLER MAQVLQGVPN
NYETDLIFPI IQAVAAIAQR DYASESESVK VSLKVIGDHL RAVTHLIADG VTASNLGRGY
VLRRLIRRVV RHGRLIGIDR PFTAEIAETA IALMAAQYPN LREREAAIKA ELTREEQRFL
ETLERGEKLL AELLAAATDQ IRGEDAFVLY DTYGFPLELT QEIAEEKGLT VDLAGFEAAM
AAQRQRSQAA HETIDLTVQG SLDRLAEQIH PSEFVGYGDA VATAKVTALL REGQSVEAAE
AGDRVQIVLD HTPFYAESGG QVGDRGVLTG ESLIVRIEDV QKESGFFVHY GQIERGLLQV
GDSVTAQIDR ACRRRAQANH TATHLLQAAL KLIVDEGISQ AGSLVAFDRL RFDFNCPRAV
TPEELRQIED QINQWIAEAH GTVVEVMPIA TAKAKGAVAM FGEKYGAEVR VIDVPGVSME
LCGGTHVANT AEIGLFKIIS EAGVASGVRR IEAVAGPAVL EYLNVRDAVV RDLSDRFKAK
PEELSDRVTA LQEELKANQK QLTALKAELA IAKSDALVSQ AIPVGDAQVL VETLTGVDAA
ALQTAAERLQ QKLGDAGAVV LGSSPEEGKV TLVAAFGPAI IAKGLKAGQF IGGIAKICGG
GGGGRPNLAQ AGGRDASKLP EAIAAALDQL KTAIAS
