ID F4P419_BATDJ Unreviewed; 415 AA.
AC F4P419;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Aminomethyltransferase {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|RuleBase:RU003981};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|RuleBase:RU003981};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395, ECO:0000256|RuleBase:RU003981};
GN ORFNames=BATDEDRAFT_16867 {ECO:0000313|EMBL:EGF79752.1};
OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF79752.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF79752.1, ECO:0000313|Proteomes:UP000007241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA Stajich J., Eisen M., Grigoriev I.V.;
RT "The draft genome of Batrachochytrium dendrobatidis.";
RL Submitted (DEC-2009) 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|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; GL882885; EGF79752.1; -; Genomic_DNA.
DR RefSeq; XP_006679387.1; XM_006679324.1.
DR AlphaFoldDB; F4P419; -.
DR STRING; 684364.F4P419; -.
DR GeneID; 18237176; -.
DR HOGENOM; CLU_007884_10_0_1; -.
DR InParanoid; F4P419; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 5473523at2759; -.
DR Proteomes; UP000007241; Unassembled WGS sequence.
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:UP000007241};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003981};
KW Transit peptide {ECO:0000256|RuleBase:RU003981}.
FT DOMAIN 41..295
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 331..408
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 415 AA; 45084 MW; 303D92B7A660D669 CRC64;
MLSTASLLRL GGKSVETTSR SQWVRCMASA PSSQPFKRTS LYDFHVKNGG KMVEFAGWDM
PVQYSSLGVL DSHLWTRKHA SIFDVSHMLQ TRWSGKDHVK FMESLVVGDI AGLQMGSSTL
SVFTNEKGGI IDDTVINRQD DKGLYVVSNA GCADKDLAHI RKQLADFQNK GGDVDVKVLD
NVSLIALQGP DAATVVQSLT KEDLSKFGFM TSRHMDIAGV DVYASRCGYT GEDGFEISVA
HKDAVALTQK LLDHPHVELA GLGARDSLRL EAGLCLYGHD LNEDITPAEG GLTWTIGKRR
RAEGGFLGAD KILSQLKVTA KGNVQLDVAN RRVGFIVSGA PAREGAEIYD KVNGTKIGTI
TSGCPSPSMM KNIGMGYIQT GFHKIGTEVQ VKVRNRFQPA VVSKMPFVAH NYFRG
//
