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Database: UniProt
Entry: A0A178IQF4_9BACT
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ID   A0A178IQF4_9BACT        Unreviewed;       377 AA.
AC   A0A178IQF4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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   ORFNames=AW736_03025 {ECO:0000313|EMBL:OAM91446.1};
OS   Opitutaceae bacterium TSB47.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX   NCBI_TaxID=1184151 {ECO:0000313|EMBL:OAM91446.1, ECO:0000313|Proteomes:UP000078486};
RN   [1] {ECO:0000313|EMBL:OAM91446.1, ECO:0000313|Proteomes:UP000078486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSB47 {ECO:0000313|EMBL:OAM91446.1,
RC   ECO:0000313|Proteomes:UP000078486};
RA   Wang Y., Shi Y., Qiu Z., Liu S., Yang H.;
RT   "High potential of lignocellulose degradation of a new Verrucomicrobia
RT   species.";
RL   Submitted (JAN-2016) 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}.
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:OAM91446.1}.
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DR   EMBL; LRRQ01000027; OAM91446.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178IQF4; -.
DR   STRING; 1184151.AW736_03025; -.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000078486; Unassembled WGS sequence.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
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   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}; Reference proteome {ECO:0000313|Proteomes:UP000078486};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          9..270
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          295..373
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   377 AA;  39765 MW;  FF689362848CD5BB CRC64;
     MSILKRTPLF DFHVAHGGRM VDFAGWEMPV QYRSILDEHK AVRRAAGLFD VSHMGEVDVR
     GPGALAFLQS LVTNDLAKMT PGRVVYSPMC GETGGVIDDL LVHMRAPGDY FLCINAGNID
     KDLAWLRERR AAAPGLDVTL ADRSGDTALI AIQGPRAAGI VRSLASGPAV AAALDDLNYY
     HFATGLTIAG IPCSAVARTG YTGEDGFELY HRPEDAPRFA EALLAAGAPL GLELAGLGAR
     DSLRLEAGFP LHGHEISGDI SPLAAGLAWT VKFAKNSDFC GRAALEREAR DGSARRVVFF
     KTGDRRIVRA GAAVIDEAGA PLGTVLSGTL SPILNEAIGS ALIDTTALAA GRALLTDIRG
     AKIALHPVKP PFVALKK
//
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