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Database: UniProt/SWISS-PROT
Entry: SYA_VIBPA
LinkDB: SYA_VIBPA
Original site: SYA_VIBPA 
ID   SYA_VIBPA               Reviewed;         860 AA.
AC   Q87LR3;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 1.
DT   26-FEB-2020, entry version 98.
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=VP2548;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC60811.1; -; Genomic_DNA.
DR   RefSeq; NP_798927.1; NC_004603.1.
DR   RefSeq; WP_005455546.1; NC_004603.1.
DR   SMR; Q87LR3; -.
DR   STRING; 223926.28807546; -.
DR   PRIDE; Q87LR3; -.
DR   EnsemblBacteria; BAC60811; BAC60811; BAC60811.
DR   GeneID; 1190072; -.
DR   KEGG; vpa:VP2548; -.
DR   PATRIC; fig|223926.6.peg.2446; -.
DR   eggNOG; ENOG4105CIM; Bacteria.
DR   eggNOG; COG0013; LUCA.
DR   HOGENOM; CLU_004485_1_1_6; -.
DR   KO; K01872; -.
DR   OMA; YHHTMFE; -.
DR   BioCyc; VPAR223926:G1GTB-2615-MONOMER; -.
DR   Proteomes; UP000002493; Chromosome 1.
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; Reference proteome; RNA-binding;
KW   tRNA-binding; Zinc.
FT   CHAIN           1..860
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000075243"
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;  93969 MW;  A85BE7D7ECFD678B CRC64;
     MYMSTDEVRN AFLKFFESKG HQIVESSSLV PHNDPTLLFT NAGMNQFKDC FLGLEKRAYT
     RATTAQRCVR AGGKHNDLEN VGFTARHHTF FEMLGNFSFG DYFKEDAISF AWEFLTDVLK
     LPADRLLVTV YETDDEAFDI WNKKVGVPAD RIIRIGDKKG GKPYESDNFW QMGDTGPCGP
     CTEIFYDHGE HIWGGRPGTP EEDGDRFIEI WNNVFMQFNR HADGTMEPLP KPSVDTGMGI
     ERISAIMQGV HSNYEIDVFQ ALIKAAAEVI GYEDLSNQSL RVIADHIRSC SFLIVDGVMP
     SNEGRGYVLR RIIRRAVRHG NKLGAQGAFF HKLVGVLADI MGTAGEELKR QQAVVEKVLR
     IEEENFGRTL ERGMAILNEA LDNLDGKVLD GETVFKLYDT YGFPADLTND VAREREFAID
     EEGFEKAMEE QRQRAREAGQ FGTDYNAAIK VDTQTEFCGY VGTKGSSSVA AMFVEGNEVD
     SLSAGDKAII VLGETPFYAE SGGQCGDAGE IRTEAGVFRV EDTQKLGNAI AHHGVMAEGV
     LAKGDEVATI VDAERRAAIS LNHSATHLLH AALRQVLGEH VTQKGSLVKA ENLRFDFSHL
     EAVTAAELKE VERLVNAQIR RNHVIETNVM DIESAKKKGA MALFGEKYDD EVRVLSMGDF
     STELCGGIHA SNTGDIGLFK ITSESGIAAG IRRIEAVTGE AALDAIEAQA AKYEEKLAES
     AQKAKTLEKE LQKLKDKMAA AESANIMGKA VEVNGTKVLV AALEGADSKN LRTMVDDIKN
     QMGSGVVLLA NVTDDKVGLI AGVTKDLVGK VKAGDLVKMV AEQVGGKGGG RPDMAQAGGT
     DVSALPEAIK TVQPWLEERL
//
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