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Database: UniProt
Entry: G5ZZH6_9PROT
LinkDB: G5ZZH6_9PROT
Original site: G5ZZH6_9PROT 
ID   G5ZZH6_9PROT            Unreviewed;       801 AA.
AC   G5ZZH6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Glycine cleavage system T protein (Aminomethyltransferase) {ECO:0000313|EMBL:EHI47861.1};
GN   ORFNames=HIMB100_00014360 {ECO:0000313|EMBL:EHI47861.1};
OS   SAR116 cluster alpha proteobacterium HIMB100.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster.
OX   NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI47861.1, ECO:0000313|Proteomes:UP000004261};
RN   [1] {ECO:0000313|EMBL:EHI47861.1, ECO:0000313|Proteomes:UP000004261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain HIMB100 {ECO:0000313|Proteomes:UP000004261};
RX   PubMed=22675578; DOI=10.4056/sigs.1854551;
RA   Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., Chen H.,
RA   D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., Logares R.,
RA   Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., Church M.J.,
RA   Steward G.F., Karl D.M., Delong E.F., Eppley J.M., Schuster S.C.,
RA   Kyrpides N.C., Rappe M.S.;
RT   "Draft genome sequence of strain HIMB100, a cultured representative of the
RT   SAR116 clade of marine Alphaproteobacteria.";
RL   Stand. Genomic Sci. 5:269-278(2011).
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:EHI47861.1}.
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DR   EMBL; AFXB01000010; EHI47861.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5ZZH6; -.
DR   STRING; 909943.HIMB100_00014360; -.
DR   PATRIC; fig|909943.3.peg.1477; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0665; Bacteria.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000004261; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR13847:SF187; DIMETHYLGLYCINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000313|EMBL:EHI47861.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004261};
KW   Transferase {ECO:0000313|EMBL:EHI47861.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..364
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          368..421
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          425..688
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          714..790
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   801 AA;  88172 MW;  1C78AF59F0709BC8 CRC64;
     MKDQYRVVVI GGGVVGASVI YHLAKFGWTD VCLLERSVLT AGSSWHAAGG IHALNADPNI
     AALQAYTIDL LQEIEEESGQ NIGLHMTGGL TMAGTEDRWE WLQAAYRVFQ SIGIDDCRLV
     TPDEARELNP IMSTDGFLGG MWADREGYLD TTGTVHAYAA AAKKRGAEYY EHTKVEALEQ
     TADGWRVITD KGTITCEHVV NAAGLWAKQV GRMAGIELPV SPLKHHYLVS DSIPQLEELD
     FEVPMTVDLE GFTYLRQDQN GVLLGIYEID HEHWAMDGAP WDYGMELFQE QTDRIEKELI
     MGFERYPVLQ DVGVKTWVNG AFTFSPDGNP LVGPVPGKKG YWCACAVMAG FLQGGGVGKS
     LAEWMIAGEP EADVYGMDVA RYGEFAENKE YIRQTTGQFY SRRFVMTYPN EQLPAGRPLK
     MAPAHDAMTA AGAQWGNSWD LEVPLYFAPQ DFTETPSLKR SNAFDLVAEE CHAVRRDVGL
     LDITGFSRFE VTGPNAESWL SRVLAARMPK PGKAALAPML SPDGRLKGDL TVFNWGDGRW
     WIMGSYYLRA WHMRWFSNYP EAGVEVRDLG EEWAGFSIAG PKSKQLIEQL TEGDIGQLGF
     MGCGMFDIGL LRTRIGRLSV AGELGYEINC RMGDHIALRR ILLAAGADCN IREYGFNAML
     SLRLEKSFGI WSAEFTQLYT PGMTGMDRFI DWKRDDFIGH KAALAEREGN GPEKKLITLS
     VQAGDADASG YEPVWSDGRL VGFVTSGGYG HTTGLSLAMA MVDTGLCAEG TNLSVHVVGV
     ERRAEVIAPS PCDPTGAVMR V
//
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