(data stored in SCRATCH zone)

SWISSPROT: D4YXR7_SPHJU

ID   D4YXR7_SPHJU            Unreviewed;       344 AA.
AC   D4YXR7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 52.
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_01445};
DE            EC=2.3.1.234 {ECO:0000256|HAMAP-Rule:MF_01445};
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000256|HAMAP-Rule:MF_01445};
DE            Short=t(6)A synthase {ECO:0000256|HAMAP-Rule:MF_01445};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000256|HAMAP-Rule:MF_01445};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000256|HAMAP-Rule:MF_01445};
GN   Name=tsaD {ECO:0000256|HAMAP-Rule:MF_01445};
GN   Synonyms=gcp {ECO:0000313|EMBL:BAI95149.1};
GN   OrderedLocusNames=SJA_C1-03150 {ECO:0000313|EMBL:BAI95149.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95149.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95149.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group
CC       on adenosine at position 37 (t(6)A37) in tRNAs that read codons
CC       beginning with adenine. Is involved in the transfer of the
CC       threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the
CC       N6 group of A37, together with TsaE and TsaB. TsaD likely plays a
CC       direct catalytic role in this reaction. {ECO:0000256|HAMAP-
CC       Rule:MF_01445, ECO:0000256|SAAS:SAAS00347456}.
CC   -!- CATALYTIC ACTIVITY: L-threonylcarbamoyladenylate + adenine(37) in
CC       tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01445, ECO:0000256|SAAS:SAAS00347377}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01445};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01445};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01445,
CC       ECO:0000256|SAAS:SAAS00347502}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01445, ECO:0000256|SAAS:SAAS00542034}.
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DR   EMBL; AP010803; BAI95149.1; -; Genomic_DNA.
DR   RefSeq; WP_013038937.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-03150; -.
DR   EnsemblBacteria; BAI95149; BAI95149; SJA_C1-03150.
DR   GeneID; 29272017; -.
DR   KEGG; sjp:SJA_C1-03150; -.
DR   eggNOG; ENOG4105CPM; Bacteria.
DR   eggNOG; COG0533; LUCA.
DR   HOGENOM; HOG000109570; -.
DR   KO; K01409; -.
DR   OMA; HLEGHIY; -.
DR   OrthoDB; POG091H010B; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase; IEA:UniProtKB-EC.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01445; TsaD; 1.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   InterPro; IPR022450; TsaD.
DR   Pfam; PF00814; Peptidase_M22; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR   TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YXR7.
DR   SWISS-2DPAGE; D4YXR7.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01445,
KW   ECO:0000256|SAAS:SAAS00425147};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01445,
KW   ECO:0000256|SAAS:SAAS00018955};
KW   Hydrolase {ECO:0000313|EMBL:BAI95149.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01445, ECO:0000256|SAAS:SAAS00019071};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01445,
KW   ECO:0000256|SAAS:SAAS00425164};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01445,
KW   ECO:0000256|SAAS:SAAS00019021};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01445,
KW   ECO:0000256|SAAS:SAAS00425140}.
FT   DOMAIN       25    306       Peptidase_M22. {ECO:0000259|Pfam:
FT                                PF00814}.
FT   REGION      135    139       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01445}.
FT   METAL       112    112       Iron. {ECO:0000256|HAMAP-Rule:MF_01445}.
FT   METAL       116    116       Iron. {ECO:0000256|HAMAP-Rule:MF_01445}.
FT   METAL       299    299       Iron. {ECO:0000256|HAMAP-Rule:MF_01445}.
FT   BINDING     168    168       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01445}.
FT   BINDING     181    181       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01445}.
FT   BINDING     185    185       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01445}.
FT   BINDING     271    271       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01445}.
SQ   SEQUENCE   344 AA;  35507 MW;  8B030732E2A17083 CRC64;
     MTIILGLESS CDETAAALVT ADGRILAHRL ATQEEAHRPY GGVVPEIAAR AHVEALAPLI
     EAALKDADLT LDDVDVIAAT AGPGLIGGVM VGLVTGKALA HAANKPLVAV NHLEGHALSP
     RLADPTLQFP YLLLLVSGGH CQLLHVRGPG DYARLATTID DASGEAFDKT AKLLGLGYPG
     GPAVEKAAAK GDPKAVPLPR PLVGTAEPHF SFAGLKSAVM RAAQSGRYST QDIAASFQQA
     VIDCLIDRTE RQLAGVQDIT ALVVAGGVAA NQSIRAALEA LAAKHDLPFV APPLWLCTDN
     AAMIAWAGAE RHAAGLIDDL TVPARPRWPL DPSAEKARGA GVKA
//

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