ID V4LXP2_9CREN Unreviewed; 371 AA.
AC V4LXP2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=MGAcid_04910 {ECO:0000313|EMBL:ESQ23721.1};
OS uncultured Acidilobus sp. MG.
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus; environmental samples.
OX NCBI_TaxID=1410573 {ECO:0000313|EMBL:ESQ23721.1, ECO:0000313|Proteomes:UP000017902};
RN [1] {ECO:0000313|EMBL:ESQ23721.1, ECO:0000313|Proteomes:UP000017902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Rusch D.B., Tringe S.G., Bailey C., Jennings R.M., Inskeep W.P.;
RT "Predominant Acidilobus-like populations from geothermal environments of
RT Yellowstone National Park exhibit similar metabolic potential in different
RT hypoxic microbial communities.";
RL Submitted (OCT-2013) 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:ESQ23721.1}.
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DR EMBL; AYMA01000001; ESQ23721.1; -; Genomic_DNA.
DR AlphaFoldDB; V4LXP2; -.
DR STRING; 1410573.MGAcid_04910; -.
DR PATRIC; fig|1410573.3.peg.467; -.
DR Proteomes; UP000017902; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..248
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 290..370
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 371 AA; 40824 MW; EF7619177C702A04 CRC64;
MSRQVPLYDV HKELGATFGE FAGWTVPMSY TSTIEEHMAV RQSAGIFDIS HMGRLRLRGP
DAAQLLDYAF TKVVSATKEG FMSGPTLALN EHARVIDDEM WYRLPSGEWL AVPNAAARER
MKSHLSWLAG LKGLKVEMED LTEALSMLAL QGPKAVEVMR ALGADWAASL RPLEFRLNVA
LAGAKAFLVS RSGWTGEDGF EVWAEHADAE KVLRAAIAAG AKLTGIAARD TLRIEMGFVL
GGNEYGEDPL KYPCALSLRY GMGAIDWSKR GFHGEEALRA CRREGLRWVR VGIEMKKSHA
RFVPRGGYKV LVDDVEVGWV TSGTFSPVLG RGIGQAYVDT RYAILGETVT VVDERGRTGE
GKLVDFPFIK K
//
