ID X5F5B3_NEIME Unreviewed; 366 AA.
AC X5F5B3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Aminomethyltransferase {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395, ECO:0000256|HAMAP-Rule:MF_00259};
GN Name=gcvT {ECO:0000256|HAMAP-Rule:MF_00259,
GN ECO:0000313|EMBL:AHW75157.1};
GN ORFNames=COH25_10420 {ECO:0000313|EMBL:RQL39116.1}, NMA510612_0855
GN {ECO:0000313|EMBL:AHW75157.1};
OS Neisseria meningitidis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487 {ECO:0000313|EMBL:AHW75157.1, ECO:0000313|Proteomes:UP000023582};
RN [1] {ECO:0000313|EMBL:AHW75157.1, ECO:0000313|Proteomes:UP000023582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=510612 {ECO:0000313|EMBL:AHW75157.1}, and NMA510612
RC {ECO:0000313|Proteomes:UP000023582};
RX PubMed=24812217;
RA Zhang Y., Yang J., Xu L., Zhu Y., Liu B., Shao Z., Zhang X., Jin Q.;
RT "Complete Genome Sequence of Neisseria meningitidis Serogroup A Strain
RT NMA510612, Isolated from a Patient with Bacterial Meningitis in China.";
RL Genome Announc. 2:e00360-14(2014).
RN [2] {ECO:0000313|Proteomes:UP000023582}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NMA510612 {ECO:0000313|Proteomes:UP000023582};
RA Zhang X., Zhang Y., Yang J., Zhu Y., Jin Q.;
RT "Complete Genome Sequence of Neisseria meningitides, serogroup A strain
RT 510612.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RQL39116.1, ECO:0000313|Proteomes:UP000284244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INS-Nm971 {ECO:0000313|EMBL:RQL39116.1,
RC ECO:0000313|Proteomes:UP000284244};
RA Duarte C., Gabastou J.M., Moreno J.;
RT "Phenotypic and genotypic characterization of Colombian isolates of
RT Neisseria meningitidis recovered from invasive disease.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000256|HAMAP-Rule:MF_00259}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00259};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|HAMAP-Rule:MF_00259}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC ECO:0000256|HAMAP-Rule:MF_00259}.
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DR EMBL; CP007524; AHW75157.1; -; Genomic_DNA.
DR EMBL; NWYP01000038; RQL39116.1; -; Genomic_DNA.
DR RefSeq; WP_002233621.1; NZ_UGRR01000006.1.
DR SMR; X5F5B3; -.
DR KEGG; nmx:NMA510612_0855; -.
DR PATRIC; fig|487.1203.peg.7; -.
DR OMA; MPVQYPA; -.
DR Proteomes; UP000023582; Chromosome.
DR Proteomes; UP000284244; Unassembled WGS sequence.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 HAMAP; MF_00259; GcvT; 1.
DR InterPro; IPR006223; GCS_T.
DR InterPro; IPR022903; GCS_T_bac.
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, ECO:0000256|HAMAP-
KW Rule:MF_00259}; Methyltransferase {ECO:0000313|EMBL:AHW75157.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00259}.
FT DOMAIN 10..258
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 285..358
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 366 AA; 39623 MW; D71A1B66EEAD4BE1 CRC64;
MITLKTTPFH QAHQDAGAKL VDFAGWELPI HYGSQIAEHE AVRTDAGMFD VSHMLVTDVA
GANAKAFFRK LIANDVAKLA FVGKALYSAL LNDNGGVIDD LIVYRTNEAE TQYRIVSNGA
TREKDTAQFH KVGQEFGVSF NPRYDLGMLA VQGPKAIEKL LTVKPEWADV VHNLKPFQGA
DLGNDWFVAR TGYTGEDGVE VILPGTEAVA FFKALQAAGV QPCGLGARDT LRMEAGMNLY
GNDMDDDTSP LEAGMGWTVD LKDESRDFVG KAALLALKEK GVAVKQVGLL LGKGGILRAH
MEVLTDKGKG ETTSGVFSPS LKQSIAIARV PKDFDGDTAK VLIRGKEADV RVLKLPFVRN
GQKQFD
//
