ID A0A0B4BJY2_9RHOB Unreviewed; 819 AA.
AC A0A0B4BJY2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Glycine cleavage system protein T {ECO:0000313|EMBL:KIC16898.1};
GN ORFNames=RA20_15875 {ECO:0000313|EMBL:KIC16898.1};
OS Leisingera sp. ANG-Vp.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1577896 {ECO:0000313|EMBL:KIC16898.1, ECO:0000313|Proteomes:UP000031177};
RN [1] {ECO:0000313|Proteomes:UP000031177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-Vp {ECO:0000313|Proteomes:UP000031177};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC16898.1}.
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DR EMBL; JWLD01000047; KIC16898.1; -; Genomic_DNA.
DR RefSeq; WP_039130849.1; NZ_JWLD01000047.1.
DR AlphaFoldDB; A0A0B4BJY2; -.
DR STRING; 1577896.RA20_15875; -.
DR OrthoDB; 9804379at2; -.
DR Proteomes; UP000031177; Unassembled WGS sequence.
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; 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;
FT DOMAIN 11..373
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 376..428
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 432..698
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 728..803
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 819 AA; 90355 MW; E2F5C05D7949002C CRC64;
MADKEFPAQA KVVIVGGGVM GVGLAYHLAH EGWGPEVVLL EKSELTSGST WHAAGQITHS
TSSFGLGKCV DYNIGLYSGK LEEETGQAVT WHGCGSFRLA YTEDEMDWLR HTLSVGRSLG
FNIELVGPEK VAELHPFYNL EGVLGALYTP DDGHVDPTNV TMAMAAGARQ KGARIIRHCR
ATNITQADNG EWIVASEKGT IRCEHVVNAG GTYARQMGEW SGLQLPMTSM THHYFVTEPV
PEFEALDKEL PVIRDDKKVS GYIRMEQKRG LIGIYEKEGS NSVWHDHCPW EYENWLFDAD
YDRVMPWLEE SLNRMPIFAD LGIQREVHGA ISHPPDGNPL IGPAPGVRNY WCCCGTQIGI
GWGPGLTREL ARWMVHGSAD ISMREYDPRR FGSYATKDWQ VTKAHEDYKL RHEIPFPHFN
RLAGRPIKPS PLYERLKEKG AVYEEVYGHE RPRWFAKNGV AQQDHYSFRR NEVHDMVGLE
CKAVREGVGI MDISAFTKVE VSGPGAAALL DRLTANRLPQ KTGGIALTHM LNRRGRIELE
TTVVKLADDS YYLVCAAFFE QRLLDHLNQN LAGEEVEITT LSTDWAALAL NGPKAREVLA
ACTDADLTNA GFKWLTAQQI EVAGHTLWAF RMSYAGELGW ELHIPRGSTL AVYDALWAAG
EAHGIADYGS FAMNAMRMEK GFKGAGELTN EVTLAEADVL RFARTDKNYL GKDKTLNDAE
KPWVCAYLEI EPDGVEDGHG GEAILLEGQV VGSTASVAYG HTVGKILAFA YVKPHANVPG
TEIEVIVAGS PRKGRILGAP AYDPESLLPR TDAALAPAE
//