ID A0A0R2Q6F3_9ACTN Unreviewed; 551 AA.
AC A0A0R2Q6F3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Glycine cleavage system protein T {ECO:0000313|EMBL:KRO45669.1};
DE Flags: Fragment;
GN ORFNames=ABR56_02975 {ECO:0000313|EMBL:KRO45669.1};
OS Acidimicrobium sp. BACL27 MAG-120823-bin4.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidimicrobium.
OX NCBI_TaxID=1655564 {ECO:0000313|EMBL:KRO45669.1, ECO:0000313|Proteomes:UP000050870};
RN [1] {ECO:0000313|EMBL:KRO45669.1, ECO:0000313|Proteomes:UP000050870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL17 MAG-120823-bin4 {ECO:0000313|EMBL:KRO45669.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KRO45669.1}.
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DR EMBL; LIAO01000330; KRO45669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2Q6F3; -.
DR Proteomes; UP000050870; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR006222; GCV_T_N.
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 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 4: Predicted;
FT DOMAIN 6..369
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 372..425
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 429..549
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT NON_TER 551
FT /evidence="ECO:0000313|EMBL:KRO45669.1"
SQ SEQUENCE 551 AA; 61097 MW; 5DFE952B220B7E74 CRC64;
MKSSARVVVI GGGVVGASVL YHLTKAGWTD VVLVERKELT AGSTWHAAGG MHTLNGDPNV
ARLQQYTVNL YKEIEKESGQ NCGIHLPGGI QLADTPERLD WLKMAHARGR YLGMKMEIIS
IKEAKVLNPL LEEKYFVGAL YDEDEGSVDP YGVTHAYAIC AKNRGAEVYT NTWVTALNHR
PDGTWDVITD KDHTIHAEHV VNAGGLWARE VGRMCGIELP VLAMEHHYLM TEPMEEVIEF
NRVNGKELPH MIDFAGEIYA RQEGQSILLG TYEQNNRPWS PKETPWDFVF QLLPHDLERI
APELERGFAH FPAVGRAGIK KFVNGPFTFS PDGNPLVGPI KGMPGMWSAC AVMAGLSQGG
GVGLSLANWM VHGDPGADIW GMDVARYGDF ATLEYTNAKV RENYSRRFRI TFPNEELAAA
RPLHTTPIYD RLLDHNAVMG AGFGLEHPLW FQDKDKEPIE DVTFYRSNAF KNVGEESRAV
RERVGFSEAS NFAKYKVSGA GSAAWLQSLF TNALPKIGRT VLTAMLNPEG KIVGEFSISR
IGEEEFFLFG S
//
