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Database: UniProt
Entry: B7ENR4_ORYSJ
LinkDB: B7ENR4_ORYSJ
Original site: B7ENR4_ORYSJ 
ID   B7ENR4_ORYSJ            Unreviewed;       409 AA.
AC   B7ENR4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
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};
DE   Flags: Fragment;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947 {ECO:0000313|EMBL:BAG94011.1};
RN   [1] {ECO:0000313|EMBL:BAG94011.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kikuchi S., Satoh K., Nagata T., Kawagashira N., Doi K., Kishimoto N.,
RA   Yazaki J., Ishikawa M., Yamada H., Ooka H., Hotta I., Kojima K., Namiki T.,
RA   Ohneda E., Yahagi W., Suzuki K., Li C., Ohtsuki K., Shishiki T., Otomo Y.,
RA   Murakami K., Iida Y., Sugano S., Fujimura T., Suzuki Y., Tsunoda Y.,
RA   Kurosaki T., Kodama T., Masuda H., Kobayashi M., Xie Q., Lu M.,
RA   Narikawa R., Sugiyama A., Mizuno K., Yokomizo S., Niikura J., Ikeda R.,
RA   Ishibiki J., Kawamata M., Yoshimura A., Miura J., Kusumegi T., Oka M.,
RA   Ryu R., Ueda M., Matsubara K., Kawai J., Carninci P., Adachi J., Aizawa K.,
RA   Arakawa T., Fukuda S., Hara A., Hashidume W., Hayatsu N., Imotani K.,
RA   Ishii Y., Itoh M., Kagawa I., Kondo S., Konno H., Miyazaki A., Osato N.,
RA   Ota Y., Saito R., Sasaki D., Sato K., Shibata K., Shinagawa A., Shiraki T.,
RA   Yoshino M., Hayashizaki Y.;
RT   "Collection, Mapping, and Annotation of Over 28,000 cDNA Clones from
RT   japonica Rice.";
RL   Science 301:376-379(2003).
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|RuleBase:RU003981}.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC       ECO:0000256|RuleBase:RU003981}.
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DR   EMBL; AK099234; BAG94011.1; -; mRNA.
DR   AlphaFoldDB; B7ENR4; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000256|RuleBase:RU003981};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003981};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003981};
KW   Transit peptide {ECO:0000256|RuleBase:RU003981}.
FT   DOMAIN          41..296
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          324..400
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
FT   NON_TER         409
FT                   /evidence="ECO:0000313|EMBL:BAG94011.1"
SQ   SEQUENCE   409 AA;  44155 MW;  A488D351AAB07A33 CRC64;
     MRGLLACATL ARRAAGATST ARRHLAGAAE AAEAELKKTA LYDFHVAHGG KMVPFAGWSM
     PIQYKDTIMD STLNCRANGS LFDVSHMCGL SLHGRQAIPF LESLVVADVA ALKDGTGTLT
     VFTNDRGGAI DDSVVTKVTD QHIYLVVNAG CRDKDLAHIG EHMEAFNKKG GDVKWHVHDE
     RSLLALQGPL AAPTLQLLTK EDLSKMYFSD FKMIDINGYA CFLTRTGYTG EDGFEISVPS
     ENAVDLAKAL LEKSEGKVRL TGLGARDSLR LEAGLCLYGN DMEQHITPVE AGLSWAIGKR
     RKAEGGFLGA DVILKQLQEG PKIRRVGLLS QGPPPRSHSE IVSNSGENIG EVTSGGFSPC
     LKKNIAMGYV KSGLHKAGTE FKVVVRGKSY DAVVTKMPFV PTKYYKPSW
//
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