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Database: UniProt
Entry: E1BB28_BOVIN
LinkDB: E1BB28_BOVIN
Original site: E1BB28_BOVIN 
ID   E1BB28_BOVIN            Unreviewed;       919 AA.
AC   E1BB28;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Sarcosine dehydrogenase {ECO:0000313|Ensembl:ENSBTAP00000005925.4};
GN   Name=SARDH {ECO:0000313|Ensembl:ENSBTAP00000005925.4,
GN   ECO:0000313|VGNC:VGNC:34289};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000005925.4, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000005925.4, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000005925.4,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000005925.4}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000005925.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   RefSeq; NP_001179970.1; NM_001193041.1.
DR   RefSeq; XP_005213422.1; XM_005213365.3.
DR   AlphaFoldDB; E1BB28; -.
DR   SMR; E1BB28; -.
DR   PaxDb; 9913-ENSBTAP00000005925; -.
DR   Ensembl; ENSBTAT00000005925.5; ENSBTAP00000005925.4; ENSBTAG00000004510.5.
DR   GeneID; 614603; -.
DR   KEGG; bta:614603; -.
DR   CTD; 1757; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004510; -.
DR   VGNC; VGNC:34289; SARDH.
DR   eggNOG; KOG2844; Eukaryota.
DR   GeneTree; ENSGT00940000157589; -.
DR   HOGENOM; CLU_007884_11_4_1; -.
DR   OMA; PMKHAYI; -.
DR   OrthoDB; 1815533at2759; -.
DR   TreeFam; TF314735; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000004510; Expressed in cortex of kidney and 94 other cell types or tissues.
DR   ExpressionAtlas; E1BB28; baseline and differential.
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; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR13847:SF200; SARCOSINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT   DOMAIN          70..428
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          431..486
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          489..798
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          824..909
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   919 AA;  100782 MW;  FD2F692E65119F10 CRC64;
     MASLSRALRG IAATRPRQSP ARGWGLRPLV SGPGPTSEKS VPYQRTLKEA EDASAAAQGP
     SQPLPGTASV VVIGGGSLGC QTLYHLAKLG VSGAVLLERE RLTSGTTWHT AGLLWQLRPS
     DVEVELLAHT RQVVSRELEE ETGLHTGWIQ NGGLFIASSQ QRLDEYKRLM SLGRVYGIES
     HVLSPGETKA LYPLMNVEDL YGTLYVPHDG TMDPAGTCTS LARAATTRGA QIIENCPVTG
     IRVRTDDFGV RRVAAVETEH GSIRTPCVIN CAGVWARAVG RMAGVNVPLV AMHHAYVVTE
     RIEGIQNMPN VRDHDASVYL RLQGDALSVG GYETNPIFCE EVSDEFAFGL FDLDWDVFTQ
     HIEGAINRVP VLEKTGIKST VCGPESFTPD HKPLMGEAPE LRGFFLGCGF NSAGMMLGGG
     CGQQLAYWIV HGRPEKDMHS YDIRRFHRSL TGHGRWIRER SHEAYAKNYS VVFPHDEPLA
     GRNMRTGPLH EELRARGCVF QERHGWERPG WFSAQGPAPV LPYDYCGAYG HRAREDYAYG
     RLLGQEYTFS FPPHHDVIKK ECLACRGAAA VFDMSYFGKF FLVGPDARKA ADWLFSADVS
     RPPGSTVYTC MLNHRGGTES DLTVSRLAPG PQASPLAPAF EGDGYYLAVG GAAAQHNWSH
     IRTVLQDRKF RCQLIDSSED LGLISVQGPA SRAVLQELLE ADLSDDAFPF STHKLVRAAG
     HLVRAVRLSF VGELGWELHA PRPSCLPVYQ ALMTAGAKHG LVNAGYRAID SLSIEKGYRH
     WHADLRADDS PLEAGLAFTC KLKSSVPFLG REALEKQRAE GLRRRLVGFT VDEKVSMFGL
     EAIWRNGQVV GHVRRADFGF TINKTLAYGY IRDPSGGPVS LDFVKSGDYA LERMGVTHAA
     QAHLKSPFDP DNKRVKGVY
//
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