OSGP2_ARATH
ID OSGP2_ARATH Reviewed; 480 AA.
AC O22145; Q8VWL2;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Probable tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03179};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=Glycoprotease 1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein GCP1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein GCP1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE Flags: Precursor;
GN Name=GCP1 {ECO:0000255|HAMAP-Rule:MF_03179}; OrderedLocusNames=At2g45270;
GN ORFNames=F4L23.22;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=19694617; DOI=10.1042/bj20091023;
RA Haussuehl K., Huesgen P.F., Meier M., Dessi P., Glaser E., Adamski J.,
RA Adamska I.;
RT "Eukaryotic GCP1 is a conserved mitochondrial protein required for
RT progression of embryo development beyond the globular stage in Arabidopsis
RT thaliana.";
RL Biochem. J. 423:333-341(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read
CC codons beginning with adenine. Probably involved in the transfer of the
CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6
CC group of A37. Involved in mitochondrial genome maintenance (By
CC similarity). May have a role in embryonic development in plants.
CC {ECO:0000255|HAMAP-Rule:MF_03179}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03179};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03179};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03179};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03179}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03179, ECO:0000269|PubMed:19694617}; Peripheral membrane
CC protein {ECO:0000269|PubMed:19694617}.
CC -!- TISSUE SPECIFICITY: Expressed in young developing leaves, roots,
CC flowers and siliques. {ECO:0000269|PubMed:19694617}.
CC -!- DEVELOPMENTAL STAGE: Expressed transiently at the early stages of
CC seedling development. Maximal expression is reached during week 3 after
CC seed germination. {ECO:0000269|PubMed:19694617}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. {ECO:0000269|PubMed:19694617}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03179}.
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DR EMBL; AY024338; AAK00530.1; -; mRNA.
DR EMBL; AC002387; AAB82636.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10532.1; -; Genomic_DNA.
DR EMBL; AY063864; AAL36220.1; -; mRNA.
DR EMBL; AY117283; AAM51358.1; -; mRNA.
DR PIR; E84888; E84888.
DR RefSeq; NP_566039.1; NM_130090.5.
DR AlphaFoldDB; O22145; -.
DR SMR; O22145; -.
DR STRING; 3702.AT2G45270.1; -.
DR PaxDb; O22145; -.
DR PRIDE; O22145; -.
DR ProteomicsDB; 248911; -.
DR EnsemblPlants; AT2G45270.1; AT2G45270.1; AT2G45270.
DR GeneID; 819135; -.
DR Gramene; AT2G45270.1; AT2G45270.1; AT2G45270.
DR KEGG; ath:AT2G45270; -.
DR Araport; AT2G45270; -.
DR TAIR; locus:2050872; AT2G45270.
DR eggNOG; KOG2707; Eukaryota.
DR HOGENOM; CLU_023208_1_1_1; -.
DR OMA; HLEGHIY; -.
DR OrthoDB; 656684at2759; -.
DR PhylomeDB; O22145; -.
DR BioCyc; ARA:AT2G45270-MON; -.
DR PRO; PR:O22145; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22145; baseline and differential.
DR Genevisible; O22145; AT.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01445; TsaD; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR022450; TsaD.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF6; PTHR11735:SF6; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transferase;
KW Transit peptide; tRNA processing.
FT TRANSIT 1..86
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT CHAIN 87..480
FT /note="Probable tRNA N6-adenosine
FT threonylcarbamoyltransferase, mitochondrial"
FT /id="PRO_0000424536"
FT BINDING 194
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 198
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 217..221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 373..374
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 401
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 402
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
SQ SEQUENCE 480 AA; 52996 MW; 20DD6A86ACC1FFAD CRC64;
MVRLFLTLSP AISRFNLYPG ISILARNNNS LRLQKHHKLK TKTPTFSLIS PSSSPNFQRT
RFYSTETRIS SLPYSENPNF DDNLVVLGIE TSCDDTAAAV VRGNGEILSQ VISSQAELLV
QYGGVAPKQA EEAHSRVIDK VVQDALDKAN LTEKDLSAVA VTIGPGLSLC LRVGVRKARR
VAGNFSLPIV GVHHMEAHAL VARLVEQELS FPFMALLISG GHNLLVLAHK LGQYTQLGTT
VDDAIGEAFD KTAKWLGLDM HRSGGPAVEE LALEGDAKSV KFNVPMKYHK DCNFSYAGLK
TQVRLAIEAK EIDAKCPVSS ATNEDRRNRA DIAASFQRVA VLHLEEKCER AIDWALELEP
SIKHMVISGG VASNKYVRLR LNNIVENKNL KLVCPPPSLC TDNGVMVAWT GLEHFRVGRY
DPPPPATEPE DYVYDLRPRW PLGEEYAKGR SEARSMRTAR IHPSLTSIIR ADSLQQQTQT
