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Database: UniProt
Entry: A0A0T2IE89_9MICO
LinkDB: A0A0T2IE89_9MICO
Original site: A0A0T2IE89_9MICO 
ID   A0A0T2IE89_9MICO        Unreviewed;       821 AA.
AC   A0A0T2IE89;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:KQZ88956.1};
GN   ORFNames=ASD62_06190 {ECO:0000313|EMBL:KQZ88956.1};
OS   Phycicoccus sp. Root563.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Phycicoccus.
OX   NCBI_TaxID=1736562 {ECO:0000313|EMBL:KQZ88956.1, ECO:0000313|Proteomes:UP000051641};
RN   [1] {ECO:0000313|Proteomes:UP000051641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root563 {ECO:0000313|Proteomes:UP000051641};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ88956.1, ECO:0000313|Proteomes:UP000051641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root563 {ECO:0000313|EMBL:KQZ88956.1,
RC   ECO:0000313|Proteomes:UP000051641};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQZ88956.1}.
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DR   EMBL; LMGM01000001; KQZ88956.1; -; Genomic_DNA.
DR   RefSeq; WP_056915210.1; NZ_LMGM01000001.1.
DR   AlphaFoldDB; A0A0T2IE89; -.
DR   STRING; 1736562.ASD62_06190; -.
DR   OrthoDB; 2055370at2; -.
DR   Proteomes; UP000051641; 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:SF193; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, 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   Reference proteome {ECO:0000313|Proteomes:UP000051641}.
FT   DOMAIN          10..367
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          370..425
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          427..698
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          724..810
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   821 AA;  88844 MW;  9924DCFEB5ABB33E CRC64;
     MTGDLPTRAR VVVIGGGVIG CSVAYHLAHL GWTDVLLLEQ GSLSGGTTWH AAGLVGQLRA
     SEAGTRLVQY STDLYARLEA ETGLGTGYRT CGGLTVARTP DRMVALRRTA ASAAAYDLDC
     ELLTADQAHE RYPLMRHEDL QGALWLPGDG RANPTDLTQA LARGARNLGV VVRERVRVTG
     VDTRDGRATG VRTDHGDVEA EVVVNCAGQW ANAVGAMAGV NVPLHSAEHF YVVTDQVDGV
     HRDLPILRDP DGWTYVKEEV GGLLVGGFEP QAKPWVPPDQ IPHPFEFALL DEDWEHFEVL
     MESAVHRLPV LAETGVRKFY NGPESFTPDN QFIIGEAPEL AGFFVAAGFN SVGIASAGGA
     GRALAEWVAE GAPTMDLISA DIRRFSPLAG NHSWLRERVV EVLGLHYAVP WPNREPETGR
     PQKRSPLHDR LVERGACLGS RNHWERANVF APQGVPPVVE YSWERPAWVD WSVSEQLATR
     SSVAVFDQTS FSKYLVTGPD AEAALQWLCT ADVAVPTGRT VYTGMLNTRG TYEADVTVTR
     LTTHEFLVVS SAATTVRDLD WIRRHVPRGS RVEVVDVTGA WAVLGVMGPL SRTLLERLTD
     DDLSDAGFPF STSREIRLGH ATVRATRITY VGELGWELYV PTELALGVHD DLFGCGADLG
     VVPAGYWTIE ALRLEKGYRA FGRELTTDLG PVEAGLTFAC KRGADHDFLG RGAVERARAE
     PPRRRVVSLV VTDPDAYLWG GELVLRDGVP VGQVTSAAWG AAVGSSVGLA LVADRQGGPV
     TAAWLTGGAW EVDLAGQRFP VRAMLRAPYD PEGLKLGRVK P
//
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