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Database: UniProt
Entry: D4GP15_HALVD
LinkDB: D4GP15_HALVD
Original site: D4GP15_HALVD 
ID   D4GP15_HALVD            Unreviewed;       837 AA.
AC   D4GP15; L9VIJ7;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Folate-binding FAD-dependent oxidoreductase {ECO:0000313|EMBL:ADE01633.1};
GN   Name=dmg1 {ECO:0000313|EMBL:ADE01633.1};
GN   OrderedLocusNames=HVO_B0014 {ECO:0000313|EMBL:ADE01633.1};
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG   Plasmid pHV3 {ECO:0000313|EMBL:ADE01633.1,
OG   ECO:0000313|Proteomes:UP000008243}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE01633.1, ECO:0000313|Proteomes:UP000008243};
RN   [1] {ECO:0000313|EMBL:ADE01633.1, ECO:0000313|Proteomes:UP000008243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC   VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; CP001953; ADE01633.1; -; Genomic_DNA.
DR   RefSeq; WP_004041140.1; NZ_AOHU01000021.1.
DR   AlphaFoldDB; D4GP15; -.
DR   PaxDb; 309800-C498_01685; -.
DR   EnsemblBacteria; ADE01633; ADE01633; HVO_B0014.
DR   GeneID; 8919270; -.
DR   KEGG; hvo:HVO_B0014; -.
DR   PATRIC; fig|309800.29.peg.323; -.
DR   eggNOG; arCOG00755; Archaea.
DR   eggNOG; arCOG00756; Archaea.
DR   HOGENOM; CLU_007884_11_2_2; -.
DR   OrthoDB; 2001at2157; -.
DR   Proteomes; UP000008243; Plasmid pHV3.
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   Plasmid {ECO:0000313|EMBL:ADE01633.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008243}.
FT   DOMAIN          14..383
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          395..446
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          448..726
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          751..829
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   837 AA;  92503 MW;  292337D320AB5218 CRC64;
     MNTWSTFPER AGTVVVGAGC VGCSAAYHLA ESGREDVVVL DRGPLFETGG STSHAPGLVF
     QTAGNKLMTE MASYTRDLYD GFGDFRTCGG IEVAYTEDRW DFLKRKREWG QSYGIDEGQL
     LTPEEVESRV PQINADVIYG GYYVPSDGKA DAVSAAESMA EEAREAGVEF YGHTEVTDID
     TTDGSVDAVE TEHGRIEADE VLVATNIWGP LFGEMVGTDI PLVPCAHQYL VSDELDELEG
     AEREIEQPLL RHQDHSLYYR QHGERYGIGS YNHESLLVDP ADIYGPDKLD DLGLEYPSLR
     EFTEEHFYEN THPDHDRSAF DAASELVPGF EDCEWTSAIN GMFSFTPDGM PILGPDEDTE
     GLWWALAVWV TQSGGAGDIV ASWMEDGTPR LDGSRVNASG AHVSRFQSHT GSREYTYGRG
     AQQYREVYQL VHPREQPDGQ RALRRSPFYD RQADLGAEFY DSDGWEVPQW YESNETLLET
     YDVPDRPDWL SQNWSKVQGA EHQHLREKVG MVDMTTFTPI EVSGPGALEF LQGLLTNDMD
     VTPGRMRYSA MLNEDGGVLA DLTVARLGDE RFVLFTGGGS SATLHSRWVT EHAPDDGSVD
     VTAHVSSRTG IGVFGPDSRK VLSDLVEADL SNDEFPFYSA QETYLGSIPV TMLRLSYAGE
     LGWEIYAPTE YGSQLWDAIR EAGEEYDIAP VGWAALDSTS MEKGFRLWGT DLTPEHNPYE
     AGIGFAADLD TDFVGKAALV ADKNDDSPSD RIVPITLDEE EAVVDAGHPV FVDDEVVGYC
     CRADYGYTID AGIAYAYLPE EYASSGQDVE IRYEGDAHPA TVRSGPLFDP DRDKMIR
//
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