ID A0A0S9C0H2_9MICC Unreviewed; 988 AA.
AC A0A0S9C0H2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Sarcosine oxidase subunit alpha {ECO:0000256|PIRNR:PIRNR037980};
DE EC=1.5.3.24 {ECO:0000256|PIRNR:PIRNR037980};
GN ORFNames=ASE96_10735 {ECO:0000313|EMBL:KQN87156.1};
OS Arthrobacter sp. Leaf69.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN87156.1, ECO:0000313|Proteomes:UP000051467};
RN [1] {ECO:0000313|EMBL:KQN87156.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN87156.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN87156.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN87156.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQN87156.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMLR01000012; KQN87156.1; -; Genomic_DNA.
DR RefSeq; WP_056430256.1; NZ_LMLR01000012.1.
DR AlphaFoldDB; A0A0S9C0H2; -.
DR STRING; 1736232.ASE96_10735; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000051467; 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 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; 2.
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 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}.
FT DOMAIN 126..398
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 492..581
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 597..867
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 891..980
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 988 AA; 104802 MW; B3617E2052C7406E CRC64;
MTSQNARLAA GGRIDRTISW RFTVDGEEFT GHPGDTLASA LLANGRITAG NSLYEDRPRG
ILAAGVEEPN ALVRVEPRFP GHVAESMLPA TTVTLVDGLK ADMLNGLGRL DPADDRAEYD
KKYVHMDVLV IGGGPAGLAA AREAARTGAR VMLMDDQPEL GGSLLSGSTS PGLAGTIEGK
PALDWVADIE AELVSGAECT VLNRTTAFGA YDANYVIAVQ NRTDHLSSPA ASGVSRQRIW
HIRANQVVLA PGAHERPLVF ENNDRPGIML ASAVRSYLNR YAVAAGQRVV IGTTNDSAYA
LAADLRAAGV KVAAVVDARP RLTDVAAAAA ESGTRVLIGS AVANTATAAS AGGGRLTSVT
VRSINDDGEL TSGVEEIACD VLAVSGGWSP LVHLHSQRQG KLRWDEDLAA FVPSTVVPNQ
QIVGSGRGSF ELVDCLAEGS SAGTAAAIAA GFSPENSNAV ADPLVLSEPK ASAPTRQLWL
VPGQTGTPDD WHHHFVDFQR DQSVADVLRS TGAGLRSVEH IKRYTSISTA NDQGKTSGVN
AIGVIAAALR HAGEASRGIG DIGTTTYRAP FTPVAFAALA GRQRGELFDP ARVTSIHPWH
VAQGALFEDV GQWKRPWYYP QNGEDMDTAV LRECAAVRES VGFMDATTLG KIEIRGKDAG
EFLNRIYTNA FKKLAPGSAR YGVMCMADGM IFDDGVTLRL DEDRYFMTTT TGGAAKVLDW
LEEWLQTEWP DLDVHCTSVT EQWTTIAVVG PKSRAVLAKV APDLAAGGGL EADAFPFMTF
RETTLASGVQ ARICRISFSG ELAYEINVPA WYGLNTWEAV AAAGAEFNIT PYGTETMHVL
RAEKGYPIVG QDTDGTVTPQ DAGMEWVVSK VKDFIGKRSY ARADAGREDR KHLVSVLPVD
GSLRLPEGSQ LVEKGITTNP AYGPVPMQGF VTSSYHSAAL GRSFALALIK NGRNRIGETL
VAAAGDQLVD VVVAETVLFD PEGTRKDG
//
