ID A0A1W7CZB5_9ACTN Unreviewed; 806 AA.
AC A0A1W7CZB5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Sarcosine dehydrogenase {ECO:0000313|EMBL:ARQ70009.1};
GN ORFNames=CAG99_15110 {ECO:0000313|EMBL:ARQ70009.1};
OS Streptomyces marincola.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2878388 {ECO:0000313|EMBL:ARQ70009.1, ECO:0000313|Proteomes:UP000194218};
RN [1] {ECO:0000313|EMBL:ARQ70009.1, ECO:0000313|Proteomes:UP000194218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 03032 {ECO:0000313|EMBL:ARQ70009.1,
RC ECO:0000313|Proteomes:UP000194218};
RA Ma L., Zhu Y., Zhang W., Zhang G., Tian X., Zhang S., Zhang C.;
RT "Complete genome sequence of Streptomyces sp. SCSIO 03032 revealed the
RT diverse biosynthetic pathways for its bioactive secondary metabolites.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CP021121; ARQ70009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W7CZB5; -.
DR KEGG; smao:CAG99_15110; -.
DR OrthoDB; 2055370at2; -.
DR Proteomes; UP000194218; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000194218}.
FT DOMAIN 8..355
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 358..412
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 416..692
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 716..798
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 806 AA; 86139 MW; 4B7BF704EE41BC6C CRC64;
MAARADTRVV IIGAGIVGCA LADELTSRGL RDVTVLDRGP LFAGPGSSYH APGLVFATSP
AKVLSDFARY TIDKYRSLGC FSPVGGLEVA TTPERLADLA RRAGLAASWG IEAERVSARR
CAELWPLLGA DRVLGGLYTP HDGLADAALA CRLQAERAMA RGATFHGGHT VTGIERGPDG
AVVAVRTDRG DVPADAVVSA AGFWGPVIGA MAGVAVPLLP LAHQYARTAP VPGLDPDARL
PILRHQDRDL YVRQHGDTLG IGSYGHRPMP VDPFTLTASE LPFSPEEFAP AWRDAAELLP
ALGGAGPPSG FDGVFSFTPD GMPLLGQVRE VPGLWLAEAV WVTHSAGAAR AVAQWLTEGR
PTTDTHLCDV HRFTGAQLSP AYITDRGAQS FVEVYDMIHP LDPPARPRPL RVGPFHVKHR
ELGAYQLEYA GWERPQWFEA NAPLAEALPP GAVPPRDAWA ARHWSPVAAA EALATRERVA
LFDMTPLTRL EVTGPGALAF LRRMTTGRVD RRPGSVGYAL LLDHGGGVRS DITVARLARD
HWQIGCNGPL DLDWLLRHAP SDGSVAVRDI TPGTCCLGVW GPLARELVAP LADADVSHEA
FGYFTARRLH IGHVPVTAMR LSYVGELGWE LYTTADLGPL LWDTLWRAGQ RLGVLAAGRA
AFTSLRLEKG YRAWGTDMTT EHDPYEAGLG FALRPGDRDF IGGAALADRS EATARRRLAC
LTLDDPAAIV LGGEPVYAAD EPARPAGYVT SAGYGHTVGR AIVYAWLPAA LAVPGTGTHV
AYFGERLAAT VRAEPLLDPE MSRIRR
//