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SYFB_GLUOX
ID   SYFB_GLUOX              Reviewed;         822 AA.
AC   Q5FUA2;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00283};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00283};
GN   Name=pheT {ECO:0000255|HAMAP-Rule:MF_00283}; OrderedLocusNames=GOX0261;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC         L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC         Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00283};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00283};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_00283};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00283}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00283}.
CC   -!- CAUTION: Lacks the conserved aspartate residue in position 480 that
CC       binds magnesium; it is replaced by a serine residue. {ECO:0000305}.
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DR   EMBL; CP000009; AAW60044.1; -; Genomic_DNA.
DR   RefSeq; WP_011251847.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FUA2; -.
DR   SMR; Q5FUA2; -.
DR   STRING; 290633.GOX0261; -.
DR   EnsemblBacteria; AAW60044; AAW60044; GOX0261.
DR   KEGG; gox:GOX0261; -.
DR   eggNOG; COG0072; Bacteria.
DR   eggNOG; COG0073; Bacteria.
DR   HOGENOM; CLU_016891_0_0_5; -.
DR   OMA; ISYNWLK; -.
DR   Proteomes; UP000006375; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00769; PheRS_beta_core; 1.
DR   CDD; cd02796; tRNA_bind_bactPheRS; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.70.380; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.50.40.10; -; 1.
DR   HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR005121; Fdx_antiC-bd.
DR   InterPro; IPR036690; Fdx_antiC-bd_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact.
DR   InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR   InterPro; IPR041616; PheRS_beta_core.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR033714; tRNA_bind_bactPheRS.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   PANTHER; PTHR10947; PTHR10947; 2.
DR   Pfam; PF03483; B3_4; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF03147; FDX-ACB; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   Pfam; PF17759; tRNA_synthFbeta; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SMART; SM00896; FDX-ACB; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54991; SSF54991; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00472; pheT_bact; 1.
DR   PROSITE; PS51483; B5; 1.
DR   PROSITE; PS51447; FDX_ACB; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; RNA-binding; tRNA-binding.
FT   CHAIN           1..822
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000232800"
FT   DOMAIN          39..150
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          399..502
FT                   /note="B5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   DOMAIN          728..821
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         486
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
FT   BINDING         490
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with alpha subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00283"
SQ   SEQUENCE   822 AA;  87792 MW;  B97E051FFA12D5DB CRC64;
     MKFSLSWLRE HLDFTASVEE ICARLNIIGL EVEGVENPAD RLVGFRTAKI VEAHRHPDAD
     RLQVCRVAAG AGFEDVQVVC GAPNARAGLH VIFATPGTYV PGLDITIKKG KIRGQDSGGM
     LCSLRELGIG EESNGIAELS ETAPIGESYA AYAELDDPVI EIAITPNRGD ALSIRGIARD
     LAAGGIGHLK PWLTEAVEGD FPSPLTWKTE HPACPYIVGR VIRGVKNGPS PDWLQRRLES
     VGVKPISALV DVTNYLTYDL GRPLHVFDVA KLKGDTLTVT HAARETFTGL DGREYVLGTE
     DMIIVDEAGV QSLAGLIGGE SSGVDENTID VFVESALFDP VRIALTGRRL AIHTDARQRF
     ERGIDPAQVL NGLEAATVMI RDLCGGEVSE ITEAGALPDW KRTARLRFER LKTLGGVDIA
     ADDTVRSLEH LGFEVTERTE DAATFLVPSW RNDIASGQVL AQAPTLDEDV ASRAASHVQA
     MEAECDLLEE VLRLYGLDNV PAVALPQTTV VPAPAVTPLQ ARAALLRRVC AARGLTETVG
     FSFVAQDDAA LFGDVPETQH LLNPIATDLD QLRPTPLINL ARALSRNLAR GLGLSGEGAL
     FEVGPSFDAT GQHLRLAGLR AGLTAREPGV AAHEATLWEA KADLTAALVA LGVPEAALSV
     TADAPGFYHP GRSGQVRQGP KMVLGTFGEL HPRVARALGL SGTVVAFEVY LDQVPLPKAK
     RKAAPVLSPL QPVRRDFAFV AGPDVEIQAV LKAARMADRN LVQDVRLFDV FEGGSLPEGH
     RSLGVEVVLQ PQSESLTDTQ LEAVSKSVEA AVLKATGAVL RR
 
 
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