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Database: UniProt
Entry: M9RH06_9RHOB
LinkDB: M9RH06_9RHOB
Original site: M9RH06_9RHOB 
ID   M9RH06_9RHOB            Unreviewed;       819 AA.
AC   M9RH06;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Sarcosine dehydrogenase {ECO:0000313|EMBL:AGI69691.1};
DE            EC=1.5.8.3 {ECO:0000313|EMBL:AGI69691.1};
GN   Name=sardh2 {ECO:0000313|EMBL:AGI69691.1};
GN   ORFNames=OAN307_c43050 {ECO:0000313|EMBL:AGI69691.1};
OS   Octadecabacter antarcticus 307.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI69691.1, ECO:0000313|Proteomes:UP000005307};
RN   [1] {ECO:0000313|EMBL:AGI69691.1, ECO:0000313|Proteomes:UP000005307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=307 {ECO:0000313|EMBL:AGI69691.1,
RC   ECO:0000313|Proteomes:UP000005307};
RX   PubMed=23671678;
RA   Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA   Brinkhoff T., Simon M., Daniel R.;
RT   "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT   Plasticity and a New Type of Xanthorhodopsin.";
RL   PLoS ONE 8:E63422-E63422(2013).
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; CP003740; AGI69691.1; -; Genomic_DNA.
DR   RefSeq; WP_015501611.1; NC_020911.1.
DR   AlphaFoldDB; M9RH06; -.
DR   STRING; 391626.OAN307_c43050; -.
DR   KEGG; oat:OAN307_c43050; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_11_0_5; -.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000005307; Chromosome.
DR   GO; GO:0008480; F:sarcosine dehydrogenase activity; IEA:UniProtKB-EC.
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:SF193; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, 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   Oxidoreductase {ECO:0000313|EMBL:AGI69691.1}.
FT   DOMAIN          12..368
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          372..426
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          428..701
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          728..811
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   819 AA;  89985 MW;  249F5A776E6F7AB3 CRC64;
     MIQDLPTHVQ TVIVGGGSIG CNTAYHLTKL GHTDVLLLER DKLTSGTTWH AAGLVVAGIL
     KSEAECEIYT HGRKLYAELE AETGLSTGFR DVGYLQIASN EERVHELRRI APFMRHHGIN
     LHEISPTQTA ELFPIADLSD VKAGFYIPED GRANPVDLTM SLAKGARMGG ARITENVTVI
     EILTKNGAAT GVRTSDGQTI TCENVVICGG MWSRQLGAAA GINLPLQAAE HYYLITDNIP
     DLPRNLPVLE DPSTYTYYRE EVGGLMLGLF EPGAAAWNLD RIPDSFAFGE IEPDWDRVGP
     HLERAYSRVP TAMDVGVRKL FCGPESFTPD LAPLVGETPE LRNCFVACGM NSLGILNGAG
     TGMVLAHWIV AGMPPIDVTA INVNRFTRSE ATRAYRCDRT PELLGKLFGQ HYPNEPPKTA
     RNVKRSVLHD RLADAGAYFT ESSGWETPDW FAPTPQQAKI ETHSWFREHW WDWHAQEHRA
     AREDVIVMDM STMSKFMVEG RDACAVLNRL SCNDVDVAVG RVVYTAWTNE RGGFEADLTV
     TRLTQDRFMV VVGENSHGHT EMRLRRTIGA DEQVIVFDAT AGITQINVHG PKARMLMEKL
     TTADMSNDAF PFMSAQEIDV GYSVVWAYRV TFVGELGWEL HVPATQAAQV YDLIVDSGRD
     FGLRNAGMQT LNSLRLEKAY RDFGLDVDNT DNPIEAGLGF AVKLDKPNGF IGRDALAAIK
     DRGVPKTRML QFLLKDPESL LHGAEMIYLN GDVVGYLQVG GYGHSLGGAV GIGFVTLDKP
     LTAQIVENGI WHVEIAGEQV SATASLKPLY DPTMSKVKS
//
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