ID A5FX79_ACICJ Unreviewed; 998 AA.
AC A5FX79;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Sarcosine oxidase, alpha subunit family {ECO:0000313|EMBL:ABQ30211.1};
GN OrderedLocusNames=Acry_0994 {ECO:0000313|EMBL:ABQ30211.1};
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ30211.1, ECO:0000313|Proteomes:UP000000245};
RN [1] {ECO:0000313|EMBL:ABQ30211.1, ECO:0000313|Proteomes:UP000000245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ30211.1,
RC ECO:0000313|Proteomes:UP000000245};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CP000697; ABQ30211.1; -; Genomic_DNA.
DR RefSeq; WP_011941913.1; NC_009484.1.
DR AlphaFoldDB; A5FX79; -.
DR STRING; 349163.Acry_0994; -.
DR KEGG; acr:Acry_0994; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_011963_0_0_5; -.
DR Proteomes; UP000000245; Chromosome.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000245}.
FT DOMAIN 172..428
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 516..597
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 905..990
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 998 AA; 106568 MW; A8C8FE8DC6FD39CB CRC64;
MSQSFRLAEG GRIDRSRTLA FRFDGRAYAG HPGDTLASAL LANGVHLVGR SFKYHRPRGI
LTAGAEEPNA LVGVGRDEGH YTPNLRATQV VLHDGLVAES QNRSPSLERD FAGLTDLFWK
FIPAGFYYKT FMWPKAAWTR FFEPRIRAMA GLGRAPEAAD AACYAQRYAH CDVLVVGAGP
AGIEAALAAA SSGARVILCD EQAELGGALL AETDATLDGT NAASFLATRL SWLQAAGQVT
ILPRTIAFGY FPHNMIGLAQ DLTDHLGEPD DTQPRGRLWQ VRAREVVIAT GAIERPLAFP
DNDRPGIMLA DAARTYVTRY GVLPGRNAVV FTAHDSAYAA ALALHRAGAR IAAIADLRPD
PSGELVEAAR AAGLPVRPGC TLTGTEGRLR VTAATIARRD GGAGERLSCD LVLMSGGFTP
SVHLFSQSRG KLRFDPALDA FIPGEPAEAC RAAGAAAGTT SLADALASGR AAGEAAAAAA
GFTAPPAAAI AVANAPAATG GFLGATPHGR NPGSVRAFID FQNDVTAKDI SLALREGFRS
VEHVKRYTTN GMATDQGKLS NMNALGIMSA ELGRPIPEIG TTTFRMPYTP VPFGYFAGYA
RGALFEPERH TPIHDWAAEQ GAVFEDVGIW KRARYFPRGG ETMRSAVARE CRAVRASVGI
FDASTLGKIE VVGPDAAEFL NRMYVNAWTK LKPGRLRYGV LLREDGFVID DGVIGRLSDT
RFHVTTTTGG APRVLAMMED YLQTEFPELD VWLTSTTEQY AVIAVQGPRA RDVIAPLVEG
ADISGAAMPH MSMVECRVAG IPARLFRVSF TGELGFEINV PADYGRAVWE AVFDAGRRHD
ITAYGTETMH VLRAEKGYII VGQETDGTAT PDDVGLAWAI GKAKPDFVGK RALDRAAFAG
QTGRKQLVGL FTEPGDIVLE EGSHLVADPS RPPPAEILGH VTSAYWSETL GRSIALALVR
GGRDRIGDTL HVKLADRAIP VRLTDPVFYD REGARLDG
//
