ID   F7X904_SINMM            Unreviewed;       997 AA.
AC   F7X904;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Sarcosine oxidase alpha subunit protein {ECO:0000313|EMBL:AEH80264.1};
GN   Name=soxA2 {ECO:0000313|EMBL:AEH80264.1};
GN   OrderedLocusNames=SM11_chr3020 {ECO:0000313|EMBL:AEH80264.1};
OS   Sinorhizobium meliloti (strain SM11).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH80264.1, ECO:0000313|Proteomes:UP000009045};
RN   [1] {ECO:0000313|EMBL:AEH80264.1, ECO:0000313|Proteomes:UP000009045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM11 {ECO:0000313|EMBL:AEH80264.1,
RC   ECO:0000313|Proteomes:UP000009045};
RX   PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA   Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA   Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT   "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT   isolate SM11 extends the S. meliloti pan-genome.";
RL   J. Biotechnol. 155:20-33(2011).
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; CP001830; AEH80264.1; -; Genomic_DNA.
DR   RefSeq; WP_010970242.1; NZ_JAJJBH010000001.1.
DR   AlphaFoldDB; F7X904; -.
DR   GeneID; 61604313; -.
DR   KEGG; smx:SM11_chr3020; -.
DR   PATRIC; fig|707241.3.peg.3152; -.
DR   HOGENOM; CLU_011963_0_0_5; -.
DR   Proteomes; UP000009045; Chromosome.
DR   GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-EC.
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   NCBIfam; TIGR01372; soxA; 1.
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; 1.
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          172..428
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          516..596
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          614..879
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          904..989
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   997 AA;  107535 MW;  E1CDAB93FF4F76E9 CRC64;
     MTGVNRISGA GRLTPARTAR FTFDGRTLTA LEGDTIASAL IANDIHLVGR SFKYHRPRGI
     LSAGAEEPNA LLDVSRDAAR RQPNVRATVQ EVFDGMKVLS QNRWPSLAFD VGGFNDLLSP
     FFAAGFYYKT FMWPKAAWHK LYEPFIRRAA GLGVAPAEPD PDHYSSRYVH CDVLVVGAGA
     AGLSAALAAA NAGAKVILCD EQPAVGGALH YDSGTMIDGK PGYDWALATG RALVAMDNVT
     LLTRTTAFGY YNHNFVGLVE RVTDHLPAPD KGLPRERLWQ VRAKKVILAN GAIERHMVFA
     NNDRPGIMLA SAGRTYLNHF GVAVGKKVGI YTAHDSAYEA AFDLRKAGID VPVIVDCRDK
     PGDMVLAEAR SLGIEVLSGH SVVNTAGKLR IASMSVARNG GGASRKIAVD ALLVSAGWTP
     SVHLFSQSRG KVTFDAATER FLPGTYAQEC LSVGACNGTD DLQATIDEAL AAGELAARAA
     GAEGGAQVAL SGRNAFEWTG GMIGAAEGAG ADKTVKAFID FQHDVCAKDI RLAVREGMHS
     IEHIKRFTTN GMASDQGKLS NMHGLAIAAE ALGKEIPQVG LTTFRQPYTP VTFGTIVSHS
     RGSLFDPARK TPIHAWEEAH GAEFEDVGNW KRAWFYPKAG ENMHEAVARE CKTVREAAGV
     FDASTLGKIE VVGPDAAEFL NLMYTNAWDN LKPGRCRYGI MLRDDGFVYD DGVVGRLAED
     RFHVTTTTGG APRVLHHMED YLQTEFPHLK VWLTSTTEQW AVIAVQGPKA REIIAPLVEG
     IDLSNEAFPH MSVAEGRICG VPTRLFRMSF TGELGFEVNV PADYGQAVWE AIWARAEPMG
     ACAYGTETMH VLRAEKGYII VGQDTDGTLT PDDAGLSWAV SKKKQDFVGI RGMKRPDLVK
     EGRKQLVGLL TKDPQVVLEE GAQIVADPNE PKPMTMLGHV TSSYWSPNCG RSIALAVVAG
     GRARLGQTLY VPMADRTIAV EVSDMVFFDK EGGRLHG
//