ID A0A0M2RDX4_9PROT Unreviewed; 383 AA.
AC A0A0M2RDX4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=aminomethyltransferase {ECO:0000256|ARBA:ARBA00012616};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395};
GN Name=gcvT {ECO:0000313|EMBL:KKJ77758.1};
GN ORFNames=WH95_04780 {ECO:0000313|EMBL:KKJ77758.1};
OS Kiloniella litopenaei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Kiloniellaceae; Kiloniella.
OX NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ77758.1, ECO:0000313|Proteomes:UP000034491};
RN [1] {ECO:0000313|EMBL:KKJ77758.1, ECO:0000313|Proteomes:UP000034491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-1 {ECO:0000313|EMBL:KKJ77758.1,
RC ECO:0000313|Proteomes:UP000034491};
RA Shao Z., Wang L., Li X.;
RT "Genome sequence of Kiloniella sp. P1-1, isolated from the gut microflora
RT of Pacific white shrimp, Penaeus vannamei.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:ARBA00001708};
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKJ77758.1}.
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DR EMBL; LANI01000003; KKJ77758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2RDX4; -.
DR STRING; 1549748.WH95_04780; -.
DR PATRIC; fig|1549748.8.peg.2438; -.
DR Proteomes; UP000034491; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000034491};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKJ77758.1}.
FT DOMAIN 26..271
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 298..375
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 383 AA; 41343 MW; 933326E2F93650AB CRC64;
MARCRCVLPY VFWSLVMSED LKKTPLYDLH VELGAKMVPF AGYSMPVQYP AGIMTEHKHT
RASAAIFDVS HMGIVRLMGD NAIPALESLL PADLENLAEN SIRYSFFTND EGGILDDLMI
TKVPGGLSLV INAACKDADI AHIKSKIGDQ VDVEVEYDNA LIALQGPKSV DVLARFDARC
ADMKFMTFMT LEIDGVSCQV SRSGYTGEDG YEIAIPAEKA VAIVRRLLDE PEVEVAGLGA
RDSLRMEAGL CLYGNDIDTT TTPIEAGLLW AIQKRRRADG GFPGDDIILK QIADGAPRRL
VGILPEGRAP LRPGVEIANA DGEVVGKVTS GGFGPSVGGP IAIAYVASDY KAPDTALNAL
VRGKEMPCKV VKMPFEQKSY FRG
//