ID F9S1B0_9VIBR Unreviewed; 372 AA.
AC F9S1B0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=VII00023_00030 {ECO:0000313|EMBL:EGU41949.1};
OS Vibrio ichthyoenteri ATCC 700023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=870968 {ECO:0000313|EMBL:EGU41949.1, ECO:0000313|Proteomes:UP000004605};
RN [1] {ECO:0000313|EMBL:EGU41949.1, ECO:0000313|Proteomes:UP000004605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700023 {ECO:0000313|EMBL:EGU41949.1,
RC ECO:0000313|Proteomes:UP000004605};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EGU41949.1}.
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DR EMBL; AFWF01000104; EGU41949.1; -; Genomic_DNA.
DR RefSeq; WP_006711881.1; NZ_AFWF01000104.1.
DR AlphaFoldDB; F9S1B0; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000004605; 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..254
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; 40127 MW; 833AB053F1E9DADF CRC64;
MTEALLNTPL HALHIEAGAK MVPFAGYDMP VQYQLGVKKE HLHTREHAGL FDVSHMGQLR
LKGAGAAAFL ETLVPVDIID LAAGNQRYAF FTNSEGGIMD DLMVANLGDH LFVVVNAACK
AHDIAHLQAH LPQGVELEVI EDRALLALQG PKAVDVLQRL QPAVAEMIFM DVGQYELLGA
QCIVSRSGYT GEDGYEISVP SEHAKALAQA LLAEEEVEWI GLGARDSLRL ECGLCLYGHD
LDETTTPVEA SLLWGIQKVR RSGEARAGGF PGADIILTQI ETKQVARKRV GLVGETKAPV
REGCELFDGD ANQIGIVTSG TAGPSAGKPV SMGYVAVEFA NIGTQVFAQV RGKMLPMTIE
KMPFVPQRYY RG
//
