ID A0A1H9DII1_9GAMM Unreviewed; 966 AA.
AC A0A1H9DII1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Sarcosine oxidase subunit alpha {ECO:0000313|EMBL:SEQ13285.1};
GN ORFNames=SAMN03080615_00572 {ECO:0000313|EMBL:SEQ13285.1};
OS Amphritea atlantica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Amphritea.
OX NCBI_TaxID=355243 {ECO:0000313|EMBL:SEQ13285.1, ECO:0000313|Proteomes:UP000198749};
RN [1] {ECO:0000313|Proteomes:UP000198749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18887 {ECO:0000313|Proteomes:UP000198749};
RA Varghese N., Submissions S.;
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; FOGB01000001; SEQ13285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9DII1; -.
DR STRING; 355243.SAMN03080615_00572; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000198749; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 1.
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; 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 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 168..422
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 497..581
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 592..855
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 879..958
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 966 AA; 106810 MW; 1BF0DF7DB8B726B6 CRC64;
MSSEKRLKAP MGLLIDREKP LSFSFEGKQY RGFAGDSIAS ALLANQQWLM SRSFKYHRPR
APLTMAGQDA NTLVQLGGEP NVLADREMIR EGISAEGQNY NGTLEGDKDA YLGHFGRFMP
VGFYYRSFFK PMGVWDKWES FIRDKAGLGK LDLTFKPEYY DKKYLFTDVV VIGSGPAGLS
AALKAADAGA KVLLVEEMPL LGGALTYNRF DIAGQQADSL RCELIDKVTA HDNIEVMTDT
VCNAWVTDNY LPLIRGKRFY KLRAKECIVA SGAYEQHVVF RNNDLPGIML CSAVTRLMKL
YAVRPGSRAV VLTGNDDGYL TALELLENGV EVAAIVDLRS EHPWPELLGA VKQKGVQVIQ
NSTVYEALPS KGNKHIRGVD IRTIVGEGEV SEFSTTLECD LLCMSAGYMP AYQLLCQAGA
QLSYNDDAAE FTLSGLPQGV HIAGSVNGLH TLEAVLNDGA NAAIRALRRL QLSDESEQPV
SCLAKPNFSW PIFSHPKGKD FVDYDEDLQA KDIVNATRLG YRDVQLVKRF STVGMGPSQG
RHSALPTARL VAKSTERTVT QTGVTTARPP FAPEKLAHVA GRIFDPRRHT AMHHRHLELG
AKMIPAGNWR RPAFYGDAAQ RDRWIREEAE HVRSRVGLID VSTLGGIEIR GADAAEFMNR
IYTFAFLKQP VGKTRYAVLT NEHGVVIDDG VACRISEDHF YVTATTSGVE RVYRDMTKWN
AQWRLDVDIL HVTSAFAAVN LAGPDARKVL QQLVDDVDLS AEAFPYLAYR EGHVAGIPAR
LLRVGFVGEL GYEIHVPTRY GEALWDALMD AGKAFDIRPF GVETQRLLRL EKGHLIVSQD
TDGMSHPGEL DLTWAVNRKK PFFVGCRSVD IVMAQPQTRK LVGFKLPLNS TKPEEGHLVL
KGDKITGNVT SCEYSSASQA IIGLAFADIA DSEPGSRISI RVEGEEIMAD VVKLPFYDPE
NLRQEM
//