ID A0A1D7YLV4_9ACTN Unreviewed; 812 AA.
AC A0A1D7YLV4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Sarcosine dehydrogenase {ECO:0000313|EMBL:AOR36531.1};
GN ORFNames=BFF78_40630 {ECO:0000313|EMBL:AOR36531.1};
OS Streptomyces fodineus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR36531.1, ECO:0000313|Proteomes:UP000094960};
RN [1] {ECO:0000313|Proteomes:UP000094960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA Kim M.-K., Kim S.B.;
RT "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL Submitted (SEP-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; CP017248; AOR36531.1; -; Genomic_DNA.
DR RefSeq; WP_069783041.1; NZ_CP017248.1.
DR AlphaFoldDB; A0A1D7YLV4; -.
DR KEGG; spun:BFF78_40630; -.
DR Proteomes; UP000094960; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
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; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 5..367
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 374..426
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 428..702
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 725..804
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 812 AA; 88931 MW; 13FE6EC152141AC0 CRC64;
MAGPRVVIIG AGVVGAALAD EISARGWTDV TVVDQGPLPA TGGSSSHAPG LVFQTNPSKT
MTELARYTVE KFCSLDVDGK PCFLQVGGLE VATSPERLTE LHRRHGWITA WGIEARLLTP
DECVAQHPLV DRDKVLGGLL VPTDGLAKAV LAVEAQIRRA TERGVRFLAR HEVLDVRQSD
GRVTGVVTDQ GELPADIVVC CAGIWGPKIA RMVGMNLPLT PLAHQLAWTG PVPALAGQTE
EAVRPILRHQ DADLYYRDRF DGLGIGYYGH RPMPVSADDI LSVDEAEEMP SVLKFTEEDF
EPAWTETQSL LPATREAKVE EGINGLFSFT TDGYPLLGQS PDVKGFWVAE AVWVTHSAGV
GRAVAEWLVD GHCSSFDLHE CDVNRFEPHQ LSPEYVLARD CQNFVEVYDI LHPLQPSGKP
RPIRTSPFHA RQQEHGAFFL EANGWERPQW YEANAALVEG RDIPTPNDWA ARYWSPIVGA
EAQVTREKVA MYDMTALKRL EVSGPGAADF LEGLVTGKVA KSVGSVTYTL LLDHDGGIRS
DITVARLARD RFQVGANGNL DLDWFTRHLP ADGRVQVRDI TAGTCCIGLW GPLAREVLQP
LTDADFSNEG LKYFRAKHVY IGSVPVTAMR LSYVGELGWE LYTTADQGQK LWDTLWAAAE
PLGGIIAGRG AFNSLRLEKG YRSFGTDMTY EHDPYEAGVG FAVKLDKGDF IGKAALERRK
TDVRRRLSCL TIDDPRAVVM GKEPVYDGDR AVGYVTSAAY GYTIGKGVAY AWLPVELAEP
GTTVHIGYFD QRVEAVVAEE PLFDPTMSRL RG
//
