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Database: UniProt
Entry: M9YB26_AZOVI
LinkDB: M9YB26_AZOVI
Original site: M9YB26_AZOVI 
ID   M9YB26_AZOVI            Unreviewed;       360 AA.
AC   M9YB26;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
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:AGK17985.1};
GN   ORFNames=AvCA6_47280 {ECO:0000313|EMBL:AGK17985.1};
OS   Azotobacter vinelandii CA6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=1283331 {ECO:0000313|EMBL:AGK17985.1, ECO:0000313|Proteomes:UP000012988};
RN   [1] {ECO:0000313|EMBL:AGK17985.1, ECO:0000313|Proteomes:UP000012988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CA6 {ECO:0000313|EMBL:AGK17985.1,
RC   ECO:0000313|Proteomes:UP000012988};
RX   PubMed=23792740; DOI=10.1128/genomeA.00313-13;
RA   Noar J.D., Bruno-Barcena J.M.;
RT   "Complete Genome Sequences of Azotobacter vinelandii Wild-Type Strain CA
RT   and Tungsten-Tolerant Mutant Strain CA6.";
RL   Genome Announc. 1:E00313-E00313(2013).
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}.
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DR   EMBL; CP005095; AGK17985.1; -; Genomic_DNA.
DR   RefSeq; WP_012703195.1; NC_021150.1.
DR   AlphaFoldDB; M9YB26; -.
DR   KEGG; avd:AvCA6_47280; -.
DR   PATRIC; fig|1283331.3.peg.4530; -.
DR   HOGENOM; CLU_007884_10_2_6; -.
DR   Proteomes; UP000012988; Chromosome.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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}; Methyltransferase {ECO:0000313|EMBL:AGK17985.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          7..253
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          280..353
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   360 AA;  39203 MW;  2E9352516F993259 CRC64;
     MGLRTPLYDQ HLALGARIVD FGGWDMPLHY GSQVEEHHQV RRDCGVFDVS HMTVVDVLGA
     DAGIWLRRLL ANDVAHLKSP GKALYSVMLN ERGGVIDDLI VYLADFGYRL VLNAATRERD
     LDWIRGQAAG FVVELRERRD LAMLAIQGPK ARARTGELLA ASRAALIHEL RPFEGLTEGD
     WFIARTGYTG EDGLEILLPA AQAPDFFNDL VGAGIAPGGL GARDTLRLEA GLNLHGREMD
     ESVSPLAANL GWTIAWDPAG RDFIGRAALE AQRRAGGQPK LVGLLLEERG VLRARQVVRV
     DGLGEGEITS GSFSPTLGKS IALARVPAAT GERAEVEIRG RWLPVRVVRP NFVRHGKALI
//
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