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Database: UniProt
Entry: A3SM72_ROSNI
LinkDB: A3SM72_ROSNI
Original site: A3SM72_ROSNI 
ID   A3SM72_ROSNI            Unreviewed;       815 AA.
AC   A3SM72;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=FAD dependent oxidoreductase/aminomethyl transferase {ECO:0000313|EMBL:EAP78453.1};
GN   ORFNames=ISM_09150 {ECO:0000313|EMBL:EAP78453.1};
OS   Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP78453.1, ECO:0000313|Proteomes:UP000005954};
RN   [1] {ECO:0000313|EMBL:EAP78453.1, ECO:0000313|Proteomes:UP000005954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-591 / DSM 15170 / ISM
RC   {ECO:0000313|Proteomes:UP000005954};
RA   Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (DEC-2005) 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:EAP78453.1}.
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DR   EMBL; AALY01000001; EAP78453.1; -; Genomic_DNA.
DR   RefSeq; WP_009813852.1; NZ_CH724156.1.
DR   AlphaFoldDB; A3SM72; -.
DR   STRING; 89187.ISM_09150; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_11_0_5; -.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000005954; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase 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: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:UP000005954};
KW   Transferase {ECO:0000313|EMBL:EAP78453.1}.
FT   DOMAIN          8..369
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          373..426
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          430..700
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          725..807
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   815 AA;  89242 MW;  BEC2BD889C2576FA CRC64;
     MSLPTQARVV IIGGGVVGCS VAYHLAKLGW KDVVLLERKQ LTSGTTWHAA GLIGQLRASQ
     NMTKLARYSA ELYKGLEAET GVATGLRQGG SVSAALTNER LEELYRQAAM ARAFGVPVEE
     LSPKEVKEKY EHINLDGVTG GVWLPTDGQA DPANIALALA KGARQNGALV KERIKVTGIK
     RKDRRVTGVD WAADDGSEQG HIACDMIVNC AGMWGHEVGR MAGVNVPLHA CEHFYIVTEG
     ISGLSQMPVL RVPDECAYYK EDAGKILLGA FEPHSKPWGM NGIPENFEFD QLPEDFDHFE
     PILEAACNRM PLLAEAGIHT FFNGPESFTP DDAYHLGLAP EMDNVWVAAG FNSIGIQSAG
     GAGHALSQWM DSGEKPFDLG DVDISRMQPF QGNKHYLFER SKETLGLLYA DHFPYLQKRT
     ARGIRRTPFH HHLLEKGAVM GEIAGWERAN WFANEGQERE YQYSWKRQNW FENARAEHMA
     IREGVGMYDM SSFGKIRVEG PDAEAFLNYV GGGDYSVPVG KIVYTQFLNS RGGIEADVTV
     TRMSETAYLV VTPAATRLAD QTWMERHKGN FNVVITDVTP GEGVLAVMGP KARDVLQAVS
     PNDFSNEVNP FGTAQEIELG MGLARVHRVT YVGELGWEIY VSADMAGHAF ETLYEAGQAH
     GLKLCGMHMM DSCRIEKGFR HFGHDITAED HVLEAGLGFA VKTAKPEFIG RDAVLRKKDE
     GLAARMVQFK LTDPEPLLYH NEPVIRDGEI VGYLSSGSYG HALGGAMGLG YVPCKGESAA
     DVLASTYEID VAGTRVRAEA SLKPMYDPKG ERAKA
//
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