ID A0A0S9CAJ0_9SPHN Unreviewed; 382 AA.
AC A0A0S9CAJ0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 ORFNames=ASE95_13485 {ECO:0000313|EMBL:KQN90674.1};
OS Sphingomonas sp. Leaf231.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736301 {ECO:0000313|EMBL:KQN90674.1, ECO:0000313|Proteomes:UP000051427};
RN [1] {ECO:0000313|EMBL:KQN90674.1, ECO:0000313|Proteomes:UP000051427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf231 {ECO:0000313|EMBL:KQN90674.1,
RC ECO:0000313|Proteomes:UP000051427};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN90674.1, ECO:0000313|Proteomes:UP000051427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf231 {ECO:0000313|EMBL:KQN90674.1,
RC ECO:0000313|Proteomes:UP000051427};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:ARBA00043710};
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:KQN90674.1}.
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DR EMBL; LMLS01000004; KQN90674.1; -; Genomic_DNA.
DR RefSeq; WP_056637756.1; NZ_LMLS01000004.1.
DR AlphaFoldDB; A0A0S9CAJ0; -.
DR STRING; 1736301.ASE95_13485; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000051427; 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:UP000051427};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..268
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 296..373
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 382 AA; 41151 MW; E6DC6B261BAADF42 CRC64;
MSDAHATQED DGFEPLEILT LPLDAWHRAR GGRMVEFAGY HMPVQYEGIM AEHLWTRENA
GLFDVSHMGQ LNITGPNVAT ALEALMPAAI HDAPLNKARY SLLLNDDGGV LDDLMLTPLG
DDRIYMVVNG ATKYDDVAHM IEHLPDDVTL NMMEDHALLA VQGPKAVEAV ARLVPGIAAL
TFMQAGAFEW NGHELWISRS GYTGEDGVEM SVPAEAVEAF ADALAAQPEI RPIGLGARDS
LRLEAGLPLY GHDLDPQTTP VQADLGFALF KRRREAADFP GATRILAERE DGPAVKRVGL
VIEGRQPVRE GADVVDASGV VVGRVTSGGF APTVGLPIAM AYVPAADAVP GQVVTLSQRG
KTHRATVTTM PFVPHRYFRG VK
//
