ID A0A0M4LND3_9GAMM Unreviewed; 805 AA.
AC A0A0M4LND3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glycine cleavage system protein T {ECO:0000313|EMBL:ALE01297.1};
GN ORFNames=W908_00955 {ECO:0000313|EMBL:ALE01297.1};
OS Candidatus Pseudothioglobus singularis PS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Pseudothioglobus.
OX NCBI_TaxID=1125411 {ECO:0000313|EMBL:ALE01297.1, ECO:0000313|Proteomes:UP000068905};
RN [1] {ECO:0000313|EMBL:ALE01297.1, ECO:0000313|Proteomes:UP000068905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS1 {ECO:0000313|EMBL:ALE01297.1,
RC ECO:0000313|Proteomes:UP000068905};
RX PubMed=26494659;
RA Marshall K.T., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus singularis' Strain PS1, a
RT Mixotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01155-e01115(2015).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CP006911; ALE01297.1; -; Genomic_DNA.
DR RefSeq; WP_053819584.1; NZ_CP006911.1.
DR AlphaFoldDB; A0A0M4LND3; -.
DR STRING; 1125411.W908_00955; -.
DR KEGG; tsn:W908_00955; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000068905; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; 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; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
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 PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000068905}.
FT DOMAIN 7..365
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 368..422
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 424..693
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 723..797
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 805 AA; 89261 MW; 477BFC52DB004DDE CRC64;
MKSHAQVVII GGGSLGVNLM YHLGLEGWTD VVLIEKGELT SGSTWHAAGL CPNFNGNHTL
SNIHEYTIKL YDEILPEKTG LPSSFHKTGS LRVGHTEVEE QWFNNIISRA NHIGCEMHFV
SKEEASIINP MMDFSSARNI LYTPNDGHVD PTTVVTQLAQ LAKKAGAEVS NFNRVTDINI
LPSGEYEVIT EQGNIIAQHV VNAGGCFSPQ VGAMVGSYVP LVNLQHQYLI TDSHPEIAAL
TKELPVTRDS IAASYIRQEG SGFLIGPYET RGSKPWALEG VDWSFDRELF EGDLERLMPW
LERCMDIFPL FKEVGISTVI NGLITHTPDD NLLVGPAKGL KNFWNLCGAS IGIAQGGIGK
YLAQWMVHGQ TELNMSSLDS RRFDTWADKN YCTTRAIESY ERMYAYAAPN DNRPHGRPIR
VSPLHTVLVQ KGAIHTVNTG FEKPSWFATD EIRGETLSWA HTEAHEAIKE ECKAVQDSCG
VTDISGTAKF RITGKDAFDF LDKLSCNKLP AKDGRIGLTL FHAPNGGIRA EQTISRISQE
EFLLMGAIGS EVKDYQWLEW HVGELDVTIE NLTEEWGGLL LTGPEARNVL SQCTQEDLSN
TGFSWLSCKT IKIDSADVFA MRVSYAGELG WELHMPSWQL ISIYESLFEM GSPFGIRDFG
GQAFNSMRLE KMYRAYGAEF TEEISALEAG MDRFLDLSRN FIGSDNIKER QSKGVETQLA
YLIFDDEIPA ECFGNEAVFD GDELSGIITS GAYGYRVSHS VAFAYLNPSH CSEGKTLRVE
TSLGSRKCHV SMNAAYDNDN EKLRS
//
