ID A0A1Z9H8A3_9PROT Unreviewed; 804 AA.
AC A0A1Z9H8A3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 03-MAY-2023, entry version 18.
DE SubName: Full=Glycine cleavage system protein T {ECO:0000313|EMBL:OUW02438.1};
GN ORFNames=CBD14_00690 {ECO:0000313|EMBL:OUW02438.1};
OS Proteobacteria bacterium TMED154.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1986844 {ECO:0000313|EMBL:OUW02438.1, ECO:0000313|Proteomes:UP000196632};
RN [1] {ECO:0000313|EMBL:OUW02438.1, ECO:0000313|Proteomes:UP000196632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED154 {ECO:0000313|EMBL:OUW02438.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OUW02438.1}.
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DR EMBL; NHHD01000006; OUW02438.1; -; Genomic_DNA.
DR Proteomes; UP000196632; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; 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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
FT DOMAIN 7..364
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 367..420
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 423..691
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 717..796
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 804 AA; 88347 MW; 416C82BA21FE9BFF CRC64;
MKTHAQVCVI GGGVVGCSVL YHLTKLGWSD VVLLERSELT SGSTWHAAGG FHTLNGDTNM
AALQGYTIKL YRELEALTGM SCGLHHVGGV TLADTSERMD MLKAERAKHR YMGLETEILS
PAEIREVAPV TNIEGVLGGL YDPLDGHLDP AGTTHAYAKA ARLNGAKIEL HTMVEQTTPR
SDGSWEVVTD KGVLIAEHVV NAGGLWAREV GAMAGVYLPL HPMEHQYVVT DDIAQIYERD
KEHPHVMDPG GESYLRQEGR GLCIGFYEQA CRPWAVDGTP WDFGHELLPD NLDKISESIA
FAYQRFPVLE TAGVKTIIHG PFTFAPDGNP LVGPVPGLRN YWSACGVMAG FXQGGGVGLT
LAQWMVEGEP DRDVXAMXVA RFGSWTNPGY TLPKVIENYQ KRFSVSYPNE ELPAARPFRT
TPVYDIQQSL GAVFGQQFGL EVANYFASED EPRYETPSFR RSNAFAATAR EVKAVRERVG
INEVQNFSKF SVTGSGARAW LDRIMAGRIP DLGRVSLAPM LSPKGRLIGD FTISCLGEEE
FQLTSSYGYQ SVHERWLRSH LEAGIDIENI SDRRTGFQIA GPMARTVLAE VTRADVSAES
FLFMDVKRMT VGMCDCIVQR LSXTGDLGYE IYTDAMDQRS LWDTLFAAGQ KHGMRPFGMR
AMMSLRLDKF FGSWLSEFSP DYTPAETGMD RFVAVNKGAD FIGRSAVEAE RQSGAARKLV
MFEVDADDAD AVGYEPVWID GEVKGFCTSG GYSHTAQKSI ALALVDDASL SDDLEAKIEI
LGDMRPAKRI HQMLFDADGA RMRG
//
