ID A0A1X3PA80_9MICC Unreviewed; 971 AA.
AC A0A1X3PA80;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Sarcosine oxidase subunit alpha {ECO:0000256|PIRNR:PIRNR037980};
DE EC=1.5.3.24 {ECO:0000256|PIRNR:PIRNR037980};
GN ORFNames=BCY76_004050 {ECO:0000313|EMBL:OSM44164.1};
OS Nesterenkonia sp. PF2B19.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Nesterenkonia.
OX NCBI_TaxID=1881858 {ECO:0000313|EMBL:OSM44164.1, ECO:0000313|Proteomes:UP000175621};
RN [1] {ECO:0000313|EMBL:OSM44164.1, ECO:0000313|Proteomes:UP000175621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF2B19 {ECO:0000313|EMBL:OSM44164.1,
RC ECO:0000313|Proteomes:UP000175621};
RX PubMed=28408669;
RA Singh P., Kapse N., Roy U., Singh S.M., Dhakephalkar P.K.;
RT "Draft Genome Sequence of Permafrost Bacterium Nesterenkonia sp. Strain
RT PF2B19, Revealing a Cold Adaptation Strategy and Diverse Biotechnological
RT Potential.";
RL Genome Announc. 5:e00133-17(2017).
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:OSM44164.1}.
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DR EMBL; MDSS02000008; OSM44164.1; -; Genomic_DNA.
DR RefSeq; WP_070162144.1; NZ_MDSS02000008.1.
DR AlphaFoldDB; A0A1X3PA80; -.
DR STRING; 1881858.BCY76_004050; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000175621; 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; 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; PF12831; FAD_oxidored; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 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 487..570
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 585..852
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 876..963
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 971 AA; 103639 MW; 3C3EA4811AA0E249 CRC64;
MTVTSRRLPA AAAPHARVET TRPRRFTLDG ETISGVQGDT VASAMLASGR LRVGDSIYLG
RPRGIFAAGV EEPNALISVR GDQPGAVTES MLSAPAVELT DGLDVRLLSG LGTLDPAADE
AYYDHKHVHT DVLVVGAGAA GLAAAREAAR SGARVMLVDE QAEAGGELLD RRSARIDGQP
ARAWITGVVG ELADSPESVH LQRTTAIGSY DANYLVAVER RRAHLSGAGA DGVSRERVWH
IRASQVVLAT GAHERHLVFA DNDRPGIMLA SAVRSYLNRY GVLAGERTVI ATTGDWVYDL
VEDLQQAGGE VAAVVDSRPE LSERALSAQA AGVPVHAGSV VAGTDADDQG DLSAVRISGL
AEDGTLTGAV TVVETDVLAL SGGFTPTIHL HTQRQGAIRW EDSLAAFVPE RPVAGQRTAG
MINGCLDLAG ALQEGADAGA AAAGDTGFAR TPQVPQADPE ALAPARPVWL VPAPGHEDLA
DAEAYRNHFV DFQRDQTVAD VMRAAGAGMR SVEHVKRYTS ISTAHDQGKT SSAALIGALA
VLLGKENPQG IGITAFRPPY TPVSFAALAG RRRGDLFDPA RITPMHSWHV AHGAVFEDVG
QWKRPWYFPQ EGESMDEAVL RECAAVRESV GFMDATTLGK IEIRGTDSGE FLNRIYTNAF
KKLAPGKARY GVMCGADGMI FDDGVTLRLD EDRYLMTTTT GGAAGVLDWL EEWLQTEWTD
LDVTCTSVTE QYATVAVAGP RSRDVIAELA PDLDVSAEAF EFMAFRETTL ASGIPARVCR
ISFSGELAFE VNVASWYGAQ VWEDIAAAGA PYGITPYGTE TMHVLRAEKG YIIVGQDTDG
TVTPQDAGME WVVSTRKDFI GKRSYARPDN QREDRKQLVS VLPADPEHRL LEGAQLIAAD
TDVAQIPVPM EGWVTSSYRS AALGRTFGLA LISRGRERIG ETLRTPVDGR LVDVLIQPTV
LYDPEGSRRD G
//
