Y1099_ARATH
ID Y1099_ARATH Reviewed; 432 AA.
AC Q681Y3; Q6NKY4; Q9C954;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Putative transferase At1g60990, chloroplastic {ECO:0000305};
DE EC=2.1.-.- {ECO:0000305};
DE AltName: Full=Iron-sulfur cluster assembly factor homolog COG0354 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At1g60990 {ECO:0000312|Araport:AT1G60990};
GN ORFNames=T7P1.13 {ECO:0000312|EMBL:AAG51655.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-432.
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=20489182; DOI=10.1073/pnas.0911586107;
RA Waller J.C., Alvarez S., Naponelli V., Lara-Nunez A., Blaby I.K.,
RA Da Silva V., Ziemak M.J., Vickers T.J., Beverley S.M., Edison A.S.,
RA Rocca J.R., Gregory J.F., de Crecy-Lagard V., Hanson A.D.;
RT "A role for tetrahydrofolates in the metabolism of iron-sulfur clusters in
RT all domains of life.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10412-10417(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21984653; DOI=10.1093/jxb/err286;
RA Waller J.C., Ellens K.W., Alvarez S., Loizeau K., Ravanel S., Hanson A.D.;
RT "Mitochondrial and plastidial COG0354 proteins have folate-dependent
RT functions in iron-sulphur cluster metabolism.";
RL J. Exp. Bot. 63:403-411(2012).
CC -!- FUNCTION: Folate-dependent protein involved in Fe/S cluster biogenesis.
CC Functionally complements an E.coli mutant defective in ygfZ.
CC {ECO:0000269|PubMed:20489182, ECO:0000269|PubMed:21984653}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21984653}.
CC -!- TISSUE SPECIFICITY: Expressed in young leaves (at protein level).
CC {ECO:0000269|PubMed:21984653}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51655.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC018908; AAG51655.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33760.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33761.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33762.1; -; Genomic_DNA.
DR EMBL; BT012559; AAS99703.1; -; mRNA.
DR EMBL; AK175484; BAD43247.1; -; mRNA.
DR PIR; E96635; E96635.
DR RefSeq; NP_001077748.1; NM_001084279.1.
DR RefSeq; NP_001117522.1; NM_001124050.2.
DR RefSeq; NP_176295.3; NM_104780.4.
DR AlphaFoldDB; Q681Y3; -.
DR SMR; Q681Y3; -.
DR STRING; 3702.AT1G60990.2; -.
DR PaxDb; Q681Y3; -.
DR PRIDE; Q681Y3; -.
DR ProteomicsDB; 242528; -.
DR EnsemblPlants; AT1G60990.1; AT1G60990.1; AT1G60990.
DR EnsemblPlants; AT1G60990.2; AT1G60990.2; AT1G60990.
DR EnsemblPlants; AT1G60990.3; AT1G60990.3; AT1G60990.
DR GeneID; 842391; -.
DR Gramene; AT1G60990.1; AT1G60990.1; AT1G60990.
DR Gramene; AT1G60990.2; AT1G60990.2; AT1G60990.
DR Gramene; AT1G60990.3; AT1G60990.3; AT1G60990.
DR KEGG; ath:AT1G60990; -.
DR Araport; AT1G60990; -.
DR TAIR; locus:2206051; AT1G60990.
DR eggNOG; KOG2770; Eukaryota.
DR HOGENOM; CLU_007884_6_3_1; -.
DR InParanoid; Q681Y3; -.
DR OMA; RHHELGP; -.
DR OrthoDB; 598391at2759; -.
DR PhylomeDB; Q681Y3; -.
DR PRO; PR:Q681Y3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q681Y3; baseline and differential.
DR Genevisible; Q681Y3; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1360.120; -; 1.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR InterPro; IPR017703; YgfZ/GcvT_CS.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR TIGRFAMs; TIGR03317; ygfZ_signature; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..432
FT /note="Putative transferase At1g60990, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433438"
SQ SEQUENCE 432 AA; 47009 MW; 6177B2EFCFFEC6F4 CRC64;
MNLLQSCKDM AMMMRIDSVS HITNTALLPC LYNGTVLRRR SLSLRKCGFR ERKFQLRCVS
ASSDSLQFDF SPPPIDHDFL DTISVSGGKV SEDGVVESFD NDDEALDAFD NGVVVVDLSH
FGRIRVSGDD RAHFLHNQTT ANFESLYEGQ GCDTVFVTPT ARTIDIAHAW IMKNAILLTV
SPTTCQSIIE MLNKYIFFAD KVEIKDITKQ TCLFALAGPK SNQIMSKLNL GDLIGQPYGR
HQHYSFDGMP ITVGVGSLIS DEGFTMLMSP GGAVSVWKTL LAEGAIPMGS VAWEKLRITQ
GRPAPERELS KEFNVLEAGL WNSISLNKGC YKGQETIARL MTYDGIKQRL CGLNLSAPSE
PGSTITVDGK KVGKLTSYTG GKNGSGHFGL GYIKKQAASI GNTVTVGEDI SGIVSEVPYL
ARQHPPSANS SS
