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
//