ID A0A1I4BKA2_9RHOB Unreviewed; 1004 AA.
AC A0A1I4BKA2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Sarcosine oxidase subunit alpha {ECO:0000313|EMBL:SFK68311.1};
GN ORFNames=SAMN04488036_1011046 {ECO:0000313|EMBL:SFK68311.1};
OS Shimia haliotis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1280847 {ECO:0000313|EMBL:SFK68311.1, ECO:0000313|Proteomes:UP000198851};
RN [1] {ECO:0000313|EMBL:SFK68311.1, ECO:0000313|Proteomes:UP000198851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28453 {ECO:0000313|EMBL:SFK68311.1,
RC ECO:0000313|Proteomes:UP000198851};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; FOSZ01000001; SFK68311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4BKA2; -.
DR STRING; 1280847.SAMN04488036_1011046; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000198851; 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; 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; 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}.
FT DOMAIN 169..421
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 620..885
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 911..996
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 1004 AA; 108247 MW; F35F2D671E46F1E4 CRC64;
MSTRLTSGGR LLNKSKQVSF SFNGKKLTGY EGDTLASALL ANDQMLMGRS FKYHRPRGVV
ASGAEEPNAL VNLGAGGKFE PNQRATTTEL YDGLSATSQN HWPSLEFDVG VANNYAARFL
PAGFYYKTFM APRAAWKHVF EPIVRQSAGL GKAPKDRDAD RYEHYYAFFD VVVVGGGVAG
LQAAKAAGQA GAKVLLMEQT AHWGGRAPVD GGEIDGKSAE DFVNATVAEL NAMDNVTIRS
RMMGAGVYDH GYMLGYERLT DHAPAVAGPR HRLWRIRAKQ IVTATGAIER PLSFAGNDIP
GVMLASAVRD YSVNFGVSSG DRTVVVTNND DAYRTAIALK NAGLEVPVIL DARATGGGAL
ADEAKALGIR VENGKAIAKV KGGKRVTGVA ICAQAGEGAV LEEIMCDAVA MSGGWSPVVH
LWSHCGGKLI WDETQAHFRP DPDRAPTSHD GNGFVVTAGT ASGPLLTGDV LADAQSAGIA
VAKAAGFDGA AGAAPSAEAQ AEAGMEPVWL MPQGAGPKLR MKAWLDYQND VKVSDVKLAA
QEGYESVEHT KRYTTLGMAT DQGKLSNING LAVLSDALNQ PIPATGTTTF RPPYTPISMG
SIAGEARDEA FQPLRRTPIH DWHEANGAFF EPVGQWRRPY CFPRGSESHA DAVTREINQT
RKSVGLLDAS TLGKIIVKGP DAGKFLDMMY TNMMSTLKPG KCRYGLMCNE NGFLIDDGVV
ARIDEDTFLC HTTTGGAERI HGWMEDWLQC EWWDWEVFTA NVTEQYAQIA VVGPNARKVI
EKLGGEMDVS KEGLAFMSWK DGKIGDFDAR AYRISFSGEL SYEIAVPASQ GRAFWDALLA
AGEEFGIMPY GTEALHVMRA EKGFIMIGDE TDGTIIPQDL NMQWAISKKK EDFLGKRAQL
RDHMASPDRW KLAGFETVDG SVIPDGSYIV ASGSNANNQR NVQGRVTSTY YSPTLDRGIA
MGLLHNALDR MGEVVEFNKV DGSTVKAKVV DPVFYDKDGE KQNV
//