ID A0A1Y0H9U0_9BACT Unreviewed; 360 AA.
AC A0A1Y0H9U0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=CCB81_11895 {ECO:0000313|EMBL:ARU44802.1};
OS Armatimonadetes bacterium Uphvl-Ar2.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=2004468 {ECO:0000313|EMBL:ARU44802.1, ECO:0000313|Proteomes:UP000195582};
RN [1] {ECO:0000313|EMBL:ARU44802.1, ECO:0000313|Proteomes:UP000195582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uphvl-Ar2 {ECO:0000313|EMBL:ARU44802.1,
RC ECO:0000313|Proteomes:UP000195582};
RA Woodhouse J.N., Makower A.K., Ionescu D., Grossart H.-P., Neilan B.A.,
RA Dittmann E.;
RT "Draft genome sequences of three Uncultured Armatimonadetes, binned from a
RT Microcystis sp. enrichment culture and from Microcystis bloom
RT metagenomes.";
RL Submitted (MAY-2017) 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}.
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DR EMBL; CP021424; ARU44802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0H9U0; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000195582; Chromosome.
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 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:UP000195582};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..257
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 282..358
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 360 AA; 38003 MW; A1C4EFF894AF237B CRC64;
MSEAARTPLY DAHVAMGGRI VTFAGYDLPV QYTGVIAESL AVRNGAGMFD VSHMARLTLS
GENVQAYLEH ITVGDIAALT DGRGHYSLLP NADGGLVDDI IVYKVRDGLF RMVVNAANHQ
KDLAHMAAQN TFGVAIEDNT ETTAMIAVQG PAALDIMAGM TPDGDKLRAL PMFGTADVTM
AGVPVFAARS GYTGEDGLEL ICSAAQSTAL WNALHAAGVT PCGLGSRDTL RVEAGLPLYG
HELKDDLSPL CAGLGWVMRK TDVPFLGRDK IEAGKAAGLP LKLHGIRLDS KRVAPIDATV
RVDGEAVGFV SSGAYSPLLE AGVAFAFLQP HIKAETACTV EIRGQEVPGQ VVNKRFFKRA
//
