ID D2S287_HALTV Unreviewed; 850 AA.
AC D2S287;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Glycine cleavage T protein (Aminomethyl transferase) {ECO:0000313|EMBL:ADB63484.1};
GN OrderedLocusNames=Htur_4706 {ECO:0000313|EMBL:ADB63484.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG Plasmid pHTUR02 {ECO:0000313|EMBL:ADB63484.1,
OG ECO:0000313|Proteomes:UP000001903}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB63484.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB63484.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RC PLASMID=pHTUR02 {ECO:0000313|EMBL:ADB63484.1,
RC ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CP001862; ADB63484.1; -; Genomic_DNA.
DR RefSeq; WP_012945728.1; NC_013745.1.
DR AlphaFoldDB; D2S287; -.
DR GeneID; 8745302; -.
DR KEGG; htu:Htur_4706; -.
DR HOGENOM; CLU_007884_11_2_2; -.
DR OrthoDB; 2001at2157; -.
DR Proteomes; UP000001903; Plasmid pHTUR02.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase 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:ADB63484.1};
KW Transferase {ECO:0000313|EMBL:ADB63484.1}.
FT DOMAIN 12..397
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 409..460
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 463..739
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 766..842
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 850 AA; 93520 MW; 40025FF5314B5CC5 CRC64;
MSTESLPSRA KTVIIGAGAV GCSIAYHLTE LGADDVVVVD QGPLPVTGGS STHAPGIMFQ
TSPSKIQTKT AHYTSRLLKD AGVYTEVGGI EVARSEERMD FLRRRVEWAT SYGLPEPQLL
EPKEVSERLP LVDEEEILGG YYSPTDGQVA GTDALQWYIE TSSARFFGDT EVTDIETGGG
EIQAVVTDNG RIECDRCVLA TNNWAYQTGQ MAGLDLPITP VEHQYVVTDP LEELRGNEDA
IGDATAGLEV PGDSQITEFM AQPPDRPVGR DQDNSLYFRT HGDGYGLGSY NHEPLVVDPD
EMGKNDEDSQ ASVHSFTEKH WTKATHPDRE KSPQQAFDEL LPATEGKDFR VTENGIFVYT
PDGMPVLGET AAVDGLWTGL AIWWTHSGGY GKILAEWMEN GVPRLPSGPV DTSGIHVNRF
EPHAGCKDYF TDRGGKRYEQ VYSIVEPRWQ PDDHRGLRVS PFYGQQQELG AEFYQSGGWE
TPQWYESNAD LVSKYEEQIP ERDGWQGVNR SPIEGAEHLH TRENVSMFDM TTFSSIMVEG
EDAGDFLQRI CSNDMDVDTG RVRYSTMLNE GGTILADITV ARLDEDEYMV TTGGGNSPGI
HGSWLQEHAP DTVSVTVEES AKCTVGLWGP KSRLLLQRVT DADVSNDEFP YFSCKRLYVG
DVPVIALRVS YVGELGWELW APSEYGQKLW NTLWEAGQDL DVRAMGGGAL ESMRLEKGFR
LWGTDIDTDV NPLEAGLPFA VDLDTEFIGK EALVEAKEEG IDTEVACLTL DDSTDVMLGG
RPVLADGEAV GYVQAGDYGY SVGESIAYTY LPSEYADAGT SVQIECEGET YDATVRDEPL
YDPGRNKIIR
//
