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Database: UniProt/SWISS-PROT
Entry: SYA_VIBC3
LinkDB: SYA_VIBC3
Original site: SYA_VIBC3 
ID   SYA_VIBC3               Reviewed;         860 AA.
AC   A5F9B7; C3LX71;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   17-JUN-2020, entry version 83.
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};
GN   OrderedLocusNames=VC0395_A0072, VC395_0562;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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}.
DR   EMBL; CP000627; ABQ21511.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP08581.1; -; Genomic_DNA.
DR   RefSeq; WP_000481018.1; NZ_CP045719.1.
DR   SMR; A5F9B7; -.
DR   STRING; 345073.VC395_0562; -.
DR   PRIDE; A5F9B7; -.
DR   EnsemblBacteria; ABQ21511; ABQ21511; VC0395_A0072.
DR   EnsemblBacteria; ACP08581; ACP08581; VC395_0562.
DR   KEGG; vco:VC0395_A0072; -.
DR   KEGG; vcr:VC395_0562; -.
DR   PATRIC; fig|345073.21.peg.551; -.
DR   eggNOG; ENOG4105CIM; Bacteria.
DR   eggNOG; COG0013; LUCA.
DR   HOGENOM; CLU_004485_1_1_6; -.
DR   KO; K01872; -.
DR   OMA; YHHTMFE; -.
DR   BioCyc; VCHO345073:G1GU4-600-MONOMER; -.
DR   Proteomes; UP000000249; Chromosome 2.
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   HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
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   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..860
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000347860"
FT   METAL           563
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   METAL           567
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   METAL           665
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   METAL           669
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   860 AA;  93827 MW;  B8BFABCBF464496A CRC64;
     MFMSTDEVRR AFLSFFESKG HQIVESSSLV PANDPTLLFT NAGMNQFKDC FLGLEKRAYT
     RATTAQRCVR AGGKHNDLEN VGFTARHHTF FEMLGNFSFG DYFKEDAIQY AWEFLTDVLQ
     LPKERLLVTV YETDDEAFDI WNKKVGIPAD RIIRIGDKKG GKKFDSDNFW QMGDTGPCGP
     CTEIFYDHGD HIWGGPPGSP EEDGDRFIEI WNNVFMQFNR HADGTMEPLP KPSVDTGMGI
     ERISAIMQGV HSNYEIDVFQ TLIKAAADAI GYQDLTNQSL RVVADHIRSC AFLIVDGVMP
     SNEGRGYVLR RIIRRAVRHG NKLGAQGAFF HKLVGPLAEV MGTAGVELKK QQALVEKVLR
     IEEENFGRTL DRGMSILNDA LDQLSGQVLD GETVFKLYDT YGFPADLTND VARERGFSID
     EAGFEQAMEE QRQRAREAGQ FGTDYNSLIK SATNTEFCGY TASRGQSVVR EMFVEGAEVS
     TLSAGDKAII VLDNTPFYAE SGGQCGDTGV LKTDAGIFHV EDTQKLGNAI AHHGVLAQGV
     LATGDQVDAI VDEKRRAAIS LNHSATHLLH AALRKVLGEH VAQKGSLVRA ETLRFDFSHL
     EAMTAAEIKE VERLVNQEVR RNHSIETNIM NIDEAKAKGA MALFGEKYDD QVRVLSMGDF
     STELCGGIHA SNTGDIGLFK IISEGGIAAG IRRIEAVTGE GALDYLDAQQ AQHDAKVSEM
     AAKAKLLEKE IQQLKDKLAA KESAGLINQV KQIAGVNVLV AQLNGADNKA LRGMVDDLKN
     QLSSGIIMLG NVAEGKVGLI AGVTNDLTNK VKAGELVNMV ALQVGGKGGG RPDMAQAGGT
     DAHALPSALE SVDAWIAERL
//
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