ID Q2BYI0_9GAMM Unreviewed; 372 AA.
AC Q2BYI0;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=SKA34_04395 {ECO:0000313|EMBL:EAR53852.1};
OS Photobacterium sp. SKA34.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=121723 {ECO:0000313|EMBL:EAR53852.1, ECO:0000313|Proteomes:UP000005284};
RN [1] {ECO:0000313|EMBL:EAR53852.1, ECO:0000313|Proteomes:UP000005284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA34 {ECO:0000313|EMBL:EAR53852.1,
RC ECO:0000313|Proteomes:UP000005284};
RA Hagstrom A.J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR53852.1}.
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DR EMBL; AAOU01000042; EAR53852.1; -; Genomic_DNA.
DR RefSeq; WP_006643849.1; NZ_CH724141.1.
DR AlphaFoldDB; Q2BYI0; -.
DR HOGENOM; CLU_007884_10_0_6; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000005284; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..255
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 287..365
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 372 AA; 40717 MW; 1B59D745985B38E1 CRC64;
MSQQLMQTPL HGLHIEMGAK MVPFAGYDMP VQYGLGVKKE HIHCRDSAGL FDVSHMGQVR
LKGQHAATLL ETLVPVDILD LPVGKQRYAV FTNENGGIED DLMVTNFGDH LFLVVNAACK
EQDIAHLKAH LKDGVELEVI EDRALLALQG PKAAMVLAEL NPTVSDMVFM DAAKMTLLDV
ECYVSRSGYT GEDGYEISVP NDKAEELARA LLAFNEVEWI GLGARDSLRL ECGLCLYGHD
LDPTTTPFEA SLMWAITPSR RAGGVREGGF PGADIILEQL QTKQVLRKRV GLVGQSKAPV
REGTKLFDAE DNEIGIVTSG TFGPTKGIPV AMGYIATEAN KLGETVYAEV RGKKLPMTIE
KMPFVPQRYY RG
//
