ID I1KNF5_SOYBN Unreviewed; 407 AA.
AC I1KNF5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Aminomethyltransferase {ECO:0000256|RuleBase:RU003981};
DE EC=2.1.2.10 {ECO:0000256|RuleBase:RU003981};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|RuleBase:RU003981};
GN Name=100778188 {ECO:0000313|EnsemblPlants:KRH51120};
GN ORFNames=GLYMA_07G262100 {ECO:0000313|EMBL:KRH51120.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH51120};
RN [1] {ECO:0000313|EMBL:KRH51120.1, ECO:0000313|EnsemblPlants:KRH51120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH51120};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH51120.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH51120}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH51120};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH51120.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH51120.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000256|RuleBase:RU003981}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + N(6)-[(R)-S(8)-
CC aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-
CC lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475,
CC Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00043710,
CC ECO:0000256|RuleBase:RU003981};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690,
CC ECO:0000256|RuleBase:RU003981}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU003981}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC ECO:0000256|RuleBase:RU003981}.
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DR EMBL; CM000840; KRH51120.1; -; Genomic_DNA.
DR EMBL; CM000840; KRH51121.1; -; Genomic_DNA.
DR RefSeq; XP_003529643.1; XM_003529595.3.
DR AlphaFoldDB; I1KNF5; -.
DR SMR; I1KNF5; -.
DR STRING; 3847.I1KNF5; -.
DR PaxDb; 3847-GLYMA07G39190-1; -.
DR EnsemblPlants; KRH51120; KRH51120; GLYMA_07G262100.
DR EnsemblPlants; KRH51121; KRH51121; GLYMA_07G262100.
DR GeneID; 100778188; -.
DR Gramene; KRH51120; KRH51120; GLYMA_07G262100.
DR Gramene; KRH51121; KRH51121; GLYMA_07G262100.
DR KEGG; gmx:100778188; -.
DR eggNOG; KOG2770; Eukaryota.
DR HOGENOM; CLU_007884_10_0_1; -.
DR InParanoid; I1KNF5; -.
DR OMA; TCTTDMA; -.
DR OrthoDB; 5473523at2759; -.
DR Proteomes; UP000008827; Chromosome 7.
DR ExpressionAtlas; I1KNF5; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 4.10.1250.10; Aminomethyltransferase fragment; 1.
DR InterPro; IPR006223; GCS_T.
DR InterPro; IPR028896; GCST/YgfZ/DmdA.
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 NCBIfam; TIGR00528; gcvT; 1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR PIRSF; PIRSF006487; GcvT; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000256|RuleBase:RU003981};
KW Mitochondrion {ECO:0000256|RuleBase:RU003981};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003981};
KW Transit peptide {ECO:0000256|RuleBase:RU003981}.
FT DOMAIN 40..295
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 323..399
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 407 AA; 44337 MW; 0429174CFCBBEBC0 CRC64;
MRGSLWQLGQ SITRRLAHGD KKAVARRCFA SEAELKKTVF HDFHVAHGGK MVPFAGWSMP
IQYKDSIMDS TINCRQNGSL FDVSHMCGLS LKGKDAVPFL EKLVIADVAG LAPGTGTLTV
FTNEKGGAID DSVITKVTDD HIYLVVNAGC RDKDLAHIEE HMKAFKAKGG DVSWHIHDER
SLLALQGPLA APVLQHLTKE DLSKLFFGEF RVLDINGSQC FLTRTGYTGE DGFEISVPSE
HGLDLAKAIL EKSEGKVRLT GLGARDSLRL EAGLCLYGND MEQHITPIEA GLTWAIGKRR
RAEGGFLGAD VILKQLEEGP KIRRVGFFSS GPPPRSHSEI QDEGGNNIGE ITSGGFSPCL
QKNIAMGYVK SGLHKAGTKV KIIIRGKPNE GVLTKMPFVP TKYYKPS
//
