ID   A0A1H7ZNS5_STRJI        Unreviewed;       950 AA.
AC   A0A1H7ZNS5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Sarcosine oxidase subunit alpha {ECO:0000256|PIRNR:PIRNR037980};
DE            EC=1.5.3.24 {ECO:0000256|PIRNR:PIRNR037980};
GN   ORFNames=SAMN05414137_13655 {ECO:0000313|EMBL:SEM60005.1};
OS   Streptacidiphilus jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptacidiphilus.
OX   NCBI_TaxID=235985 {ECO:0000313|EMBL:SEM60005.1, ECO:0000313|Proteomes:UP000183015};
RN   [1] {ECO:0000313|Proteomes:UP000183015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45096 / BCRC 16803 / CGMCC 4.1857 / CIP 109030 / JCM 12277
RC   / KCTC 19219 / NBRC 100920 / 33214
RC   {ECO:0000313|Proteomes:UP000183015};
RA   Varghese N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
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; FOAZ01000036; SEM60005.1; -; Genomic_DNA.
DR   RefSeq; WP_042458055.1; NZ_FOAZ01000036.1.
DR   AlphaFoldDB; A0A1H7ZNS5; -.
DR   STRING; 235985.SAMN05414137_13655; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0446; Bacteria.
DR   OrthoDB; 5287468at2; -.
DR   Proteomes; UP000183015; 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; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR042204; 2Fe-2S-bd_N.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
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; 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   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:UP000183015}.
FT   DOMAIN          120..370
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          465..548
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          564..829
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          854..942
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   950 AA;  100847 MW;  95D979DC0F72D241 CRC64;
     MSSRLPTGGR VDRSAPLRFT FDGVEYPGLS GDTLASALIA NGVLTVGPSL YRERPRGVVT
     AGVDDPHALV QLERPQNEPM QLATTVELCD GLVATGLQGR GRLEEEPDEA LFDKTYLHTD
     VLVVGAGPAG LAAALAAGRS GARVVLVDDQ PELGGALLGG REEIDGRPGP AWVAEVRAEL
     ETQPETRVLT RATAIGYHDR NYVLVAERRP DRPGGGGRLW HLRARQVVLA TGAHERPLVF
     AGNDRPGVMA AAAVRTYLGR YAVLPGRRAV VFTTGDSAYA TALELAAAGA VVPALVDTRP
     EPPAALVEAA RAAGIEVLAG SAVVGTEGEE RLTGVRVSAL TDDGQLTGAV QELACDLLAV
     SGGWSPAVHL WSMARGTVRY DEALAAFVPD RAAQDVRTAG SARGRHDLAG CLTEGLTAGA
     EAATAAGFPV EVPATPSCTG DEPPAAPRPV WLVPGESGDP STWRDHFVDT QRDATVADVH
     RAVRAGMRSV EHIKRYTTIG TAHDQGKSCG VAAIGVIAQL LGARSPGEVG TTTYRGPYVP
     VSFALLAGRE RGPLFDPVRT TPVHPWHVRR GAVFENVGQW HRPRYYPRPG EDMDAAVLRE
     CRAAREGVAM MDASTLGKID VIGPDAGVFL DRLYTNGFAK LPVGSARYGV MCRADGMVFD
     DGVTVRLAPD HYYLTTTTGN AAAVLDWMEE WLQTEWPELR VSCTSVTEQW TTVAVVGPRS
     REVLAALAPG LDVSNEAFPF MTVRHTELAN GLPARICRIS FSGELSYEVN VAGWYGLALW
     EAVLAYGAHA GITPYGTETM HVLRAEKGYP IVGQDTDGTV TPQDLGMSWI VARHKDFVGR
     RSFARADTSR VDRKHLVGLL PVDRAELLPE GAQLVAPGTD VTAVPAESLG HVTSSYRSAA
     LGRTFALALV RGGRDRIGDT VLAPLPDGRT VAATVTEPVL FDPKGTRRDG
//