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Database: UniProt
Entry: S4MPH3_9ACTN
LinkDB: S4MPH3_9ACTN
Original site: S4MPH3_9ACTN 
ID   S4MPH3_9ACTN            Unreviewed;      1115 AA.
AC   S4MPH3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Putative Sarcosine oxidase subunit alpha {ECO:0000313|EMBL:EPJ35332.1};
GN   ORFNames=STAFG_7617 {ECO:0000313|EMBL:EPJ35332.1};
OS   Streptomyces afghaniensis 772.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ35332.1, ECO:0000313|Proteomes:UP000015001};
RN   [1] {ECO:0000313|EMBL:EPJ35332.1, ECO:0000313|Proteomes:UP000015001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=772 {ECO:0000313|EMBL:EPJ35332.1,
RC   ECO:0000313|Proteomes:UP000015001};
RA   Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA   Goodfellow M., Mueller M.;
RT   "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT   Compounds of the Julimycin B-Complex.";
RL   Submitted (FEB-2013) 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:EPJ35332.1}.
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DR   EMBL; AOPY01001645; EPJ35332.1; -; Genomic_DNA.
DR   RefSeq; WP_020276451.1; NZ_KE354420.1.
DR   AlphaFoldDB; S4MPH3; -.
DR   PATRIC; fig|1283301.3.peg.7559; -.
DR   HOGENOM; CLU_011963_0_0_11; -.
DR   OrthoDB; 5287468at2; -.
DR   Proteomes; UP000015001; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.30.2270.10; Folate-binding superfamily; 1.
DR   InterPro; IPR042204; 2Fe-2S-bd_N.
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; IPR006279; SoxD.
DR   InterPro; IPR038561; SoxD_sf.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   NCBIfam; TIGR01372; soxA; 1.
DR   NCBIfam; TIGR01374; soxD; 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   Pfam; PF04267; SoxD; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
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:UP000015001}.
FT   DOMAIN          298..557
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          634..715
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          730..996
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          1021..1107
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
FT   REGION          107..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1115 AA;  119183 MW;  95D7D0979264FBE8 CRC64;
     MLLIPCPWCG PRDEAEFHYG GQAHVPYPQD PSSLTDEDWA RYLFFRDNPR GPFAERWTHA
     SGCRRWFNAV RDTSTNEILT VYRAGEERPA TFESRQVHPA RPALEDEAVQ AEAGSGAAAP
     VEVRGAQPPL GSGPGAAAPV GVQGAQPPRG SGGAAPSGVE GAEPLEDRTG RGGGGEETQP
     FRHPTRGRIH RDTPLTFTFD GTAYQGYKGD TLASALLANG VIQTGTSIKL GRPRGIFSAG
     VEEPNAVVQI EAPFPEPMLP ATTVELYDGL VATGLPGQGR LATAPDPARY DAVHAHCDLL
     VVGAGPAGLA AAAAAARSGA RVILADDQPE PGGSLLGTGE LLDWVDDTTA RLDAAPDVRV
     LRRTTVFGYY DDNHLLAVER RTNHLGAEAP EHVSRERVWR IRARRVVLAT GAHERSLAFA
     DNDRPGVMLA ASARAYVNRH GVLPGRHAVV FTTNDSAYAA ALDLAAAGVA VEAVVDTRAE
     PGEWAERARQ AGIEVLTGHA VTGTEGAPRL TSVTVAPYGE TTGRREFAAD LLLVSGGWNP
     VAHLFSQAGG KLRHDEELGT FVPDTCRQAV EVAGGASGAF ELARVLAQGA AAGARALQAE
     GYTCESPRLP QVATPPQTPP MRVFTIPSRE GAPRFVDLQR DVTVDDLARA TGAGMRSVEH
     TKRYTTAGTA NDQGKTSGVL ASGVVAELLG VDVSALGTTT FRPPYTPVSF AALAGRDRGA
     LLDPIRTTAL HEWHVAHGAL FENVGQWKRP WYYPQDGEDM ETAVLRECAA AREGVAFMDA
     STLGKIDVQG PDAGVFLDLL YTNMMSTLKV GMIRYGVMCR PDGMVFDDGT VIRLDQDRYL
     VTTTTGNAAA VLDWMEEWLQ TEWPELRVHC TSVTEQWATV ALVGPRSREV LGSLAPRLAV
     ANEDFPFMAW RETTVAGIEA RVCRISFSGE LAYEINVSPW EALALWEALY EAGAPYGITP
     YGTETMHVLR AEKGYPIVGQ DTDGTVTPQD LGMSWVVSKK KRDFIGKRSH ARADTARPDR
     KHLVGLLPED PGTFLPEGTH LVAGSVLPAP PVPMLGHVTS SYRSAALGRT FALALVKGGR
     DRIGERLYAP VGDRLVPVTV ASPVLYDPEG ARRDG
//
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