ID A0A2S8EPX2_9RHOB Unreviewed; 1003 AA.
AC A0A2S8EPX2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Sarcosine oxidase subunit alpha family protein {ECO:0000313|EMBL:PQO21892.1};
GN ORFNames=C2I36_15895 {ECO:0000313|EMBL:PQO21892.1};
OS Rhodobacteraceae bacterium WD3A24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2086263 {ECO:0000313|EMBL:PQO21892.1, ECO:0000313|Proteomes:UP000237945};
RN [1] {ECO:0000313|EMBL:PQO21892.1, ECO:0000313|Proteomes:UP000237945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WD3A24 {ECO:0000313|EMBL:PQO21892.1,
RC ECO:0000313|Proteomes:UP000237945};
RA Wang S.;
RT "The draft genome sequence of Pararoseibaca halophilus WD3A24.";
RL Submitted (JAN-2018) 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:PQO21892.1}.
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DR EMBL; PUHN01000083; PQO21892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8EPX2; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000237945; 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 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; 1.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000237945}.
FT DOMAIN 170..422
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 522..604
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 619..884
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 910..995
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
FT REGION 923..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 109299 MW; 21FBC279EEA133D3 CRC64;
MSTRLATGGR LIDRSARRRF TFDGRAHEGY AGDTLASALL AGGHTLLGRS FKYHRPRGLV
ASGAEEPNAL VGLGAGARFE PNQRATTTEL FDGLQAVSQN AWPSLDWDVG VVNNAFARFL
PAGFYYKMFM HPRPLWKHLF EPFIRRSAGL GRAPSERDAD RYEHFYAFCD VLVVGGGIAG
LQAALAAGRA GARVILLEQT AHWGGRSPVD GVRIDGGPAE AWINAAVQEL DGMENVTLRP
RTMGAGVYDH GYVLGYERVG DHDPAAEVPR HRLWRIRAAR LITATGALER PLSFAGNDVP
GVMLASAVRD YVVNWAVSPG DRTVVVTNND DAYRTALALK SAGLEVPAIL DARPRAEGEL
PEMARAHGIR VETGKGVAKV RGGRHVTAVG VCAQAGEGAV LEEIACDAVA MSGGWSPVVH
LWSHCGGKLE WDAAQALFRP DPDRAPTGHD GHPFVATAGA ASGALQADRA MADADENMKN
VLQGIGRKSP SRKPPKVESA EEAPLAPVWQ MPQGAGPALR AKMWLDYQND VKVSDVRLAA
QEGYESVEHT KRYTTLGMAT DQGKLSNING LATLSQALHE EIPQVGTTTF RPPYTPISMA
AIAGEARGPV FQPLRRTPMH EWHEANGADW EPVGQWRRPY CYRRAGESRR DAVHREVRNT
RNALGLLDAS TLGKIMVSGP DAERFIDMLY TGKMSTLKPG KCRYGLMCDE NGFLMDDGVC
ARLDERSFLC HTTSGGAERI HGWMEDWLQC EWWDWQVHVV NLTEQFAQVA VVGPNARNLL
ERLGGIDVSK ETLPFMAWTE GTLGGFRARV FRISFSGELS FEIAVPASEG RAFWERLVEA
GEGFGAMPYG TEALHVMRAE KGFIMIGDET DGTIIPQDLG LDWAISKKKE DFLGKRGMER
VNMTSPDRWK LVGLETLDGS VLPDGAHAPA EGLNANGQRN TQGRVTSTYY SPTLGRGIAM
ALVHRGPERM GETIAFNVPG RTPVKAKIVE PVFYDPKGER QNV
//