ID   D8UF24_VOLCA            Unreviewed;       420 AA.
AC   D8UF24;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
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   ORFNames=VOLCADRAFT_107582 {ECO:0000313|EMBL:EFJ41696.1};
OS   Volvox carteri f. nagariensis.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX   NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN   [1] {ECO:0000313|EMBL:EFJ41696.1, ECO:0000313|Proteomes:UP000001058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX   PubMed=20616280; DOI=10.1126/science.1188800;
RA   Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA   Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA   Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA   Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA   Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT   "Genomic analysis of organismal complexity in the multicellular green alga
RT   Volvox carteri.";
RL   Science 329:223-226(2010).
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; GL378391; EFJ41696.1; -; Genomic_DNA.
DR   RefSeq; XP_002957198.1; XM_002957152.1.
DR   AlphaFoldDB; D8UF24; -.
DR   STRING; 3068.D8UF24; -.
DR   GeneID; 9626693; -.
DR   KEGG; vcn:VOLCADRAFT_107582; -.
DR   eggNOG; KOG2770; Eukaryota.
DR   InParanoid; D8UF24; -.
DR   OrthoDB; 5473523at2759; -.
DR   Proteomes; UP000001058; Unassembled WGS sequence.
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   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:UP000001058};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003981};
KW   Transit peptide {ECO:0000256|RuleBase:RU003981}.
FT   DOMAIN          49..303
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          330..406
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   420 AA;  45040 MW;  3BD75DAF6787EE0D CRC64;
     MSSTRRLLTL LPQLGRAGAL RASEHASATG SLLFTRGFAD DANLKKTVLY DFHVANGGKM
     VPFAGWSMPI QYKDSIMEST IFCRKNASLF DVSHMCGLTL KGKDAIKFLE GLVVGDIAGL
     KDGTGSLSVF TNEQGGIIDD TVITKVNGQE IYVVVNAGCR DKDLAHLDKH LQAAKSKGLD
     VALTVHDDRS LLALQGPAAK DVLGALAPGV DLAAMYFSDF RTFDVAGIPC WVTRTGYTGE
     DGFEISVPST HAVALAEKLT ASERVRLAGL GPRDSLRLEA GLCLYGNDLN ESLTPVEAGL
     AWTIGKRRRE GFDFLGGDVI KKQLAEGVSK RRVGFVSSGA PARQHSVIST PDGQVVGEVT
     SGAFSPCLKK NIAMGYVEKD FSKPGTQLKV EVRGKQNEAV VTKMPFLPTP YYKRPEAAKK
//