ID   A0A495RL77_SPHMI        Unreviewed;       960 AA.
AC   A0A495RL77;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Sarcosine oxidase subunit alpha {ECO:0000313|EMBL:RKS88292.1};
GN   ORFNames=DFR51_2940 {ECO:0000313|EMBL:RKS88292.1};
OS   Sphingosinicella microcystinivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingosinicellaceae; Sphingosinicella.
OX   NCBI_TaxID=335406 {ECO:0000313|EMBL:RKS88292.1, ECO:0000313|Proteomes:UP000276029};
RN   [1] {ECO:0000313|EMBL:RKS88292.1, ECO:0000313|Proteomes:UP000276029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19791 {ECO:0000313|EMBL:RKS88292.1,
RC   ECO:0000313|Proteomes:UP000276029};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (OCT-2018) 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:RKS88292.1}.
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DR   EMBL; RBWX01000009; RKS88292.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495RL77; -.
DR   OrthoDB; 5287468at2; -.
DR   Proteomes; UP000276029; Unassembled WGS sequence.
DR   GO; GO:0008115; F:sarcosine oxidase activity; IEA:InterPro.
DR   GO; GO:0046653; P:tetrahydrofolate metabolic process; IEA:InterPro.
DR   Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR042204; 2Fe-2S-bd_N.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
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; IPR006277; Sarcosine_oxidase_asu.
DR   InterPro; IPR041117; SoxA_A3.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF17806; SO_alpha_A3; 1.
DR   PIRSF; PIRSF037980; SoxA; 2.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          167..424
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          479..561
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          576..839
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          867..952
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   960 AA;  103005 MW;  C27DAB2484CA83C2 CRC64;
     MSGYRLGHGG DIDRTRPITF QWEGRNYSGF AGDTLASALL ASGVRMMGRS FKYHRPRGLI
     AAGLDEPNAI VQLEQGAQTI PNLKAPYIDL YDGLSANPVN AWPSLGFDLL AVNGLVKRFI
     PAAFYYKTFM WPDWLLFEPS IRKAAGLGTS PTLPDPDVYT QTSAHTDVLV VGGGIAGLSA
     ALQAAQTGKS VMLVTGGAHW GGRLAATSDT IEGKPARVWI EDTLQTLAAM PNITLMARTL
     ATGHYDHGMV ALCERLTDHL PLEQRSGPRQ RLWRVRTDEL ILATGAIERP LVFRGNDRPG
     VMLAGAARAY LHRYGVVAGR RIVVATNNDS AWQAAFDLAD AGAHLVAIVD ARNAPPTVLI
     ERAQSLGIPV HSGTAPAAAL GGRALRGVRI GRVSEGGHIG GATQKLRCDT LLVSGGWNPA
     VHLHSHGAGR LALDANLHSF TPIAAAGHRS VGGAAGDFAP PSPIPALWSI SESGAPDPEA
     WVDFQNDVTA GDVALAAREN FRSVEHLKRY TTLGMASDQG KTSNVNGIGI LSTVLDKPMQ
     AIGTTKFRPP YDPTPFGVFA GHRVGEGLRP RRRLALHDWH TEHGAALDEY GGWMRPAAYP
     RSSEGEETAV RREVLAVRSS VGLFEASPLG KVEVKGPDAA AFLDRMYVNT ISTLKPGRCR
     YAIMLTENGT VFDDGVVTRL ADDHFLGGTT SGHAAAVAEA FREWLQCEWI TMQVLVEDVT
     TCWAVANIAG PKARDVLSAL EPDMDISSTA FPHMSARTGH VCSLPARIAR VSFTGELSYE
     IAVPWRDAGR LWTALVEAGA PHGMTPFGVE ALMTMRIEKG FLHVGSDTDG TTLPQDIGFG
     GIMQKKKQDF VGRRSALRPD GMRDDRRSLV GLEITDGKSV PLATGAHVLP ATAAGEQPSQ
     GWVTSSTWSP TLNAPLAFAL IERGQERMGE TVRVWDLGTW REARITGLCR YDPEGARLDA
//