ID A0A1S9MEN2_9MICC Unreviewed; 981 AA.
AC A0A1S9MEN2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Sarcosine oxidase subunit alpha {ECO:0000256|PIRNR:PIRNR037980};
DE EC=1.5.3.24 {ECO:0000256|PIRNR:PIRNR037980};
GN ORFNames=BMF89_06105 {ECO:0000313|EMBL:OOP63549.1};
OS Arthrobacter sp. SRS-W-1-2016.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1930254 {ECO:0000313|EMBL:OOP63549.1, ECO:0000313|Proteomes:UP000190514};
RN [1] {ECO:0000313|EMBL:OOP63549.1, ECO:0000313|Proteomes:UP000190514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS-W-1-2016 {ECO:0000313|EMBL:OOP63549.1,
RC ECO:0000313|Proteomes:UP000190514};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + O2 + sarcosine = (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate + glycine + H2O2;
CC Xref=Rhea:RHEA:70455, ChEBI:CHEBI:15379, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:57305, ChEBI:CHEBI:57433,
CC ChEBI:CHEBI:57453; EC=1.5.3.24;
CC Evidence={ECO:0000256|PIRNR:PIRNR037980};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|PIRNR:PIRNR037980};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRNR:PIRNR037980};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037980}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC ECO:0000256|PIRNR:PIRNR037980}.
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:OOP63549.1}.
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DR EMBL; MTPV01000024; OOP63549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9MEN2; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000190514; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IEA:UniProtKB-UniRule.
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; 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; 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; 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 Cytoplasm {ECO:0000256|PIRNR:PIRNR037980};
KW NAD {ECO:0000256|PIRNR:PIRNR037980};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037980};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR037980};
KW Reference proteome {ECO:0000313|Proteomes:UP000190514}.
FT DOMAIN 127..400
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 485..574
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 590..859
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 884..973
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 981 AA; 104204 MW; 3A405B5DCD661C5B CRC64;
MTPQNARLAT GGRIDRSISW RFTVDGQEFT GHPGDTVASA LLANGRINAG NSLYEDRARG
IMSAGVEESN ALVKVAARFP GHVAESMLPA TTVSLVDGLS VEFLNGLGRL DPNEDRAEYD
KKYVHTDVLV VGGGVSGLAA AREAVRTGAR VILIDDQPEL GGSQLSGSTA PELAEVIEGK
QALEWIADVE AELVSAAECT VLNRTTAFGS YDANYVIAAQ NRTDHLGSPA ADGVSRQRIW
HIRAKQVVLA PGAHERPLVF ENNDRPGIML ASAVRSYLNR YAVAAGRRVV IGTTNDSAYL
LAADLLAAGV KVAAVVDARP KLSDKAAAAV ESGIRVLVGS AVADTSGAGE NGRIDAVTIR
SLNDDGEVTS GVERLACDLL AVSGGWSPVV HLHSQRQGKV RWDDDLAAFV PSSVVKDQHV
VGAGRGSYGL ADCLGEGVSA GAAAAIAAGF SSETVPAEIK APVASAPTRQ LWLVPGQSGN
AGEWHHHFVD FQRDQSVADV LRSTGAGMRS VEHIKRYTSI STANDQGKTS GVNAIGVIAA
ALKQAGEASR GIGDIGTTTY RAPFTPVAFA ALAGRQRGEL FDPARVTSIH PWHVAQGALF
EDVGQWKRPW YYPQAGEDMD AAVLRECAAV RESVGFMDAT TLGKIEIRGK EAGEFLNRIY
TNAFKKLAPG SARYGVMCTP DGMIFDDGVT LRLDEGRYFM TTTTGGAAKV LDWLEEWHQT
EWPELDVVCT SVTEQWTTIA VVGPKSRAVI AKVAPQLAAD GGLDAEAFPF MTFRETTLAS
GVQARICRIS FSGELAYEIN VPSWYGLDTW ESVAAAGAEF NITPYGTETM HVLRAEKGYP
IVGQDTDGTV TPQDAGMEWI VSKAKDFIGK RSYSREDAVR TDRKHLVSVL PADGSFRLPE
GTQLVEKGIP VNPAYGPVPM QGFVTSSYHS AALGRSFGLA LITNGRNRIG ETLVASVGDQ
LLDVVVGETV LFDAEGTRKD G
//
