ID A0A101KTJ5_RHILI Unreviewed; 815 AA.
AC A0A101KTJ5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:KUM26724.1};
GN ORFNames=AU467_20210 {ECO:0000313|EMBL:KUM26724.1};
OS Rhizobium loti (Mesorhizobium loti).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=381 {ECO:0000313|EMBL:KUM26724.1, ECO:0000313|Proteomes:UP000053176};
RN [1] {ECO:0000313|EMBL:KUM26724.1, ECO:0000313|Proteomes:UP000053176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFLA 01-765 {ECO:0000313|EMBL:KUM26724.1,
RC ECO:0000313|Proteomes:UP000053176};
RA Rangel W.M., Thijs S., Longatti S.M., Moreira F.M., Weyens N.,
RA Vangronsveld J., Van Hamme J.D., Bottos E.M., Rineau F.;
RT "Draft genome sequence of Mesorhizobium sp. UFLA 01-765, a multitolerant
RT efficient symbiont and plant-growth promoting strain isolated from Zn-
RT mining soil using Leucaena leucocephala as a trap plant.";
RL Submitted (DEC-2015) 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:KUM26724.1}.
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DR EMBL; LPWA01000103; KUM26724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101KTJ5; -.
DR OrthoDB; 9804379at2; -.
DR Proteomes; UP000053176; 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; 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:SF9; SARCOSINE DEHYDROGENASE; 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 11..369
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 372..427
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 429..700
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 724..807
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 815 AA; 90417 MW; 6F9F522183A77779 CRC64;
MTKTVPNKAR AVIIGGGVSG CSVAYHLAKL GWTDIVLLER KQLTSGTTWH AAGLIGQLRA
SQNMTRLAKY SADLYVKLEA ETEVGTGMRQ VGSITVALTE ERKHEIYRQA SLARAFDVDV
REISPREVSE MYPHLNVSDV VGAVHLPLDG QCDPANIAMA LAKGARQRGA TVIENVKVTK
VHTKNGRVSG VSWAQGEDLG TIETDIVVNC AGMWARELGR QNGVTIPLHA CEHFYLVTEP
IPGLSRLPVL RVPDECAYYK EDAGKMMLGA FEPVAKPWGM DGIREDFCFD QLPEDMDHFE
PILEMGINRM PMLGTAGIHT FFNGPESFTP DDRYYLGEAP ELAGYWMATG YNSIGIVSSG
GAGMALAQWI NDGEAPFDLW EVDIRRAQPF QKNRRYLKER VSETLGLLYA DHFPYRQMAT
SRGVRRSSLH EHLKARGAVF GEVAGWERAN WFARDGQERE YRYSWKRQNW FDNQREEHLA
VRNGVGLFDM TSFGKIRVEG RDACAFLQKL CANDMDVAPG KIVYTQMLNQ RGGIESDLTV
TRLSETAYFL VVPGATLQRD LAWLRRHVAD EFVVITDVTA AEAVICVMGP EARKLIQKVS
PNDFSNEANP FGTFQEIEIG MGLARAHRVT YVGELGWELY VSTEQAAHVF EAITEAGADI
GLKLCGLHTL DSCRIEKAFR HFGHDITDED NVLEAGLGFA VKTSKADFIG RDAVLRKKEA
GLSRRLVQFR LKDSQPLLFH NEAILRDGRI VGPITSGNYG HHLGGAIGLG YVPCHGESEA
DVLGSSYEVE IAGERFAAEA SLKPMYDPRA ERVKR
//