ID   F6EPI7_HOYSD            Unreviewed;       812 AA.
AC   F6EPI7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Putative dehydrogenase {ECO:0000313|EMBL:AEF39420.1};
GN   OrderedLocusNames=AS9A_0968 {ECO:0000313|EMBL:AEF39420.1};
OS   Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS   (Amycolicicoccus subflavus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC   Hoyosella.
OX   NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF39420.1, ECO:0000313|Proteomes:UP000009235};
RN   [1] {ECO:0000313|EMBL:AEF39420.1, ECO:0000313|Proteomes:UP000009235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX   PubMed=21725023; DOI=10.1128/JB.05388-11;
RA   Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA   Wu X.L.;
RT   "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT   actinomycete isolated from crude oil-polluted soil.";
RL   J. Bacteriol. 193:4538-4539(2011).
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; CP002786; AEF39420.1; -; Genomic_DNA.
DR   RefSeq; WP_013805769.1; NC_015564.1.
DR   AlphaFoldDB; F6EPI7; -.
DR   STRING; 443218.AS9A_0968; -.
DR   KEGG; asd:AS9A_0968; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_11_2_11; -.
DR   OrthoDB; 2055370at2; -.
DR   Proteomes; UP000009235; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT   DOMAIN          6..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          429..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;  88848 MW;  C3B693ED968AA69C CRC64;
     MSGRRTVIIG AGVVGAAIAD ELSALGWTDI VVVDQGDFPA TGGSTSHAPG VVFQANGSKA
     MTDLARYTVE KFVALEHQGE SCFLQVGGLE VATTPERMAE IHRRHGWLTS WGVEAEVVDA
     DRCVELHPLL DGTRVLGGLH CPTDGLAKAL WAVEAQIERA MSRGVRMLPR HEVLDITVEN
     GKVVGVVTNH GEIPADVVVC CAGIWGPKVA ALVGMNLPLT PLAHQLAWTG SIPALAGQTD
     EAVRPALRHQ DADLYFRDRY DQLAIGYYGH RPMPIDANGL LSVDDAAVMP SVLEFTPSDF
     GPAWEETQAL LPSTTEAKIE EGINGVFSFT PDGMPLLGES QDVSGFWVAE AVWVTHSAGV
     GRAMAEWLAN GYSSSFDLHE CELNRFEDFQ LLPEFVLERD CQNFVEVYDI LHPLQPMDSP
     RGIRTSPFYP RQQELDAFFL PATGWERPHW YNSNKDLLDR FQVPQPNDWA ARYWSPIVGA
     EAQATRDSVA MYDMTALKRL TVTGSGATAF LQRLTTGTID KSIGSVTYTL LLDHDGGIRS
     DVTIARLGEH HYQVGANGAL DTNWFHRFLP QDGSVTVTDI TPGTCCIGLW GPKAREVLSQ
     LTDADLTNTG LKFFRAAQIN IGNVPVTAMR LSYVGELGWE LYTTADLGLR LWDTLWEAGQ
     NHGIIAAGRG AFNSLRLEKG YRSFGTDMTF EHDPYEAGVG FAVKLDKGDF IGRDALLRRK
     ENQTRTLACL TIDNHVDVVA GKEPVFLNDR PVGYVTSAAY GYTINKGIAY AWLPTEAATP
     GTEVEIGYFG RRIRAVVTAE PLFDPKMTRL RG
//