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Database: UniProt
Entry: A0A2T1DKH3_9CYAN
LinkDB: A0A2T1DKH3_9CYAN
Original site: A0A2T1DKH3_9CYAN 
ID   A0A2T1DKH3_9CYAN        Unreviewed;       374 AA.
AC   A0A2T1DKH3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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   ECO:0000313|EMBL:PSB20955.1};
GN   ORFNames=C7B65_06005 {ECO:0000313|EMBL:PSB20955.1};
OS   Phormidesmis priestleyi ULC007.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Phormidesmis.
OX   NCBI_TaxID=1920490 {ECO:0000313|EMBL:PSB20955.1, ECO:0000313|Proteomes:UP000238634};
RN   [1] {ECO:0000313|EMBL:PSB20955.1, ECO:0000313|Proteomes:UP000238634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULC007 {ECO:0000313|EMBL:PSB20955.1,
RC   ECO:0000313|Proteomes:UP000238634};
RA   Cohen D.B., Kent A.D.;
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PSB20955.1, ECO:0000313|Proteomes:UP000238634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULC007 {ECO:0000313|EMBL:PSB20955.1,
RC   ECO:0000313|Proteomes:UP000238634};
RA   Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT   "The ancient ancestry and fast evolution of plastids.";
RL   Submitted (MAR-2018) 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:PSB20955.1}.
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DR   EMBL; PVWG01000004; PSB20955.1; -; Genomic_DNA.
DR   RefSeq; WP_073070672.1; NZ_PVWG01000004.1.
DR   AlphaFoldDB; A0A2T1DKH3; -.
DR   STRING; 1920490.GCA_001895925_03581; -.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000238634; 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   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   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:UP000238634};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          18..266
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          292..369
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   374 AA;  40699 MW;  A87FE2A6285113F3 CRC64;
     MTDPTKTPDL LARTSLFALA VELRARMTGF SGWEMPVQFS GIGQEHQAVR TAAGMFDISH
     MGKFALKGKD VLSQIQTLVP SDLSRLQIGQ AQYTVLLNPE GGIIDDLIFY YQGILDGDQR
     WMIIVNAATT LKDKTWMLEH LDLSQMSFED YSLSKALIAV QGPDAVRHLQ ALVDADLSPI
     KAFGHLEANV LGQPAFLART GYTGEDGFEV MLDPEVAIEL WRSLLASGVT PCGLGARDTL
     RLEAAMALYG QDIDDTTTPL EAGLGWLVHL DTKGDFIGRS ALEQQKKSGV TKRLVGLQMQ
     GRNIARHHYP VLHDGQAVGI VTSGTLAPTV GCAIALAYVP IALAQVGQSV EVEIRGKNYP
     AIVVKRPFYR AKKV
//
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