ID F7Y5V3_MESOW Unreviewed; 366 AA.
AC F7Y5V3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 OrderedLocusNames=Mesop_4075 {ECO:0000313|EMBL:AEH88509.1};
OS Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=536019 {ECO:0000313|EMBL:AEH88509.1, ECO:0000313|Proteomes:UP000001623};
RN [1] {ECO:0000313|EMBL:AEH88509.1, ECO:0000313|Proteomes:UP000001623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24607 / HAMBI 3007 / WSM2075
RC {ECO:0000313|Proteomes:UP000001623};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Mavrommatis K.M., Tiwari R.P.,
RA Howieson J.G., O'Hara G.W., Nandasena K.G., Woyke T.;
RT "Complete sequence of Mesorhizobium opportunistum WSM2075.";
RL Submitted (OCT-2010) 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; CP002279; AEH88509.1; -; Genomic_DNA.
DR RefSeq; WP_013895189.1; NC_015675.1.
DR AlphaFoldDB; F7Y5V3; -.
DR STRING; 536019.Mesop_4075; -.
DR KEGG; mop:Mesop_4075; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_0_5; -.
DR Proteomes; UP000001623; 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 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 11..254
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 366 AA; 39126 MW; CB5AA4207264AAFA CRC64;
MTGDDSRHLP LEDIHAAAGA RFGAFAGWSM PLTYPAGVMK EHLHTREHAG LFDISHMKLF
EVSGPQAVAL LDRACPLDAG ALEISQSKLS FFLNEAGGIL DDLIITRLGD ARFMVVANAG
NAVADEKHLR DLAKDFDATV EPLDRVFLAI QGPEAWAVLS RAGIETGSLL FMHGVEPRKS
WFMSRSGYTG EDGFEIGLPV TDARDLVTKL LEDERVLWIG LAARDSLRLE AGLCLHGQDI
TPETDPAAAA LMWAIPKEIR ATGAFIGADA LRAAVERGPT QKRVGLKPEG RQPVRAGAAL
FDADGNPAGH VTSGGFGPSA GHPVAMGYVA TPLAKPGTRL FADVRGTKIP VDISSLPFTP
HRYRKG
//
