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Database: UniProt
Entry: A0A011ALU5_9ACTN
LinkDB: A0A011ALU5_9ACTN
Original site: A0A011ALU5_9ACTN 
ID   A0A011ALU5_9ACTN        Unreviewed;       889 AA.
AC   A0A011ALU5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Glycine cleavage system T protein (Aminomethyltransferase) {ECO:0000313|EMBL:EXG82916.1};
GN   ORFNames=CryarDRAFT_4120 {ECO:0000313|EMBL:EXG82916.1};
OS   Cryptosporangium arvum DSM 44712.
OC   Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC   Cryptosporangiaceae; Cryptosporangium.
OX   NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG82916.1, ECO:0000313|Proteomes:UP000021053};
RN   [1] {ECO:0000313|EMBL:EXG82916.1, ECO:0000313|Proteomes:UP000021053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG82916.1,
RC   ECO:0000313|Proteomes:UP000021053};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXG82916.1}.
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DR   EMBL; JFBT01000001; EXG82916.1; -; Genomic_DNA.
DR   RefSeq; WP_051570705.1; NZ_KK073874.1.
DR   AlphaFoldDB; A0A011ALU5; -.
DR   PATRIC; fig|927661.3.peg.4093; -.
DR   HOGENOM; CLU_011963_0_0_11; -.
DR   OrthoDB; 5287468at2; -.
DR   Proteomes; UP000021053; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR042204; 2Fe-2S-bd_N.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
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; IPR041117; SoxA_A3.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF17806; SO_alpha_A3; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:EXG82916.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000021053};
KW   Transferase {ECO:0000313|EMBL:EXG82916.1}.
FT   DOMAIN          118..362
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          410..491
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          506..772
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          797..881
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   889 AA;  95776 MW;  EC014C90C23736B9 CRC64;
     MRARTGGRID RGRTLTFTFD GETYTGHPGD TLASALLAAG RHTIARSITF GRPRGITAAW
     AEDSGGPVQI EEPFPEPMRP ATTVELYDGL SARSLAGRGR LADVPDTARY DAKHHHVDVL
     VVGAGPAGLA AARDAARAGD RVALVDEQSE AGGSLLSEPE TPGWVADTVA ELAAHPDVLH
     LQRTTAFGTY DDGFVLALER RTDHLGAAAP KNVSRQRVWR LRARRIVVAT GAHERPIVFA
     DNDRPGIMLA GAARTFLNRY GVLPGRAAVV FTTNDSAYDA AFDLHRAGVR VRAIVDARTE
     IPAHLAEACD RARIWLVRGA VVTGTRGEDR ITHALVGPDP IACDLLLVSG GWNPAVHLFS
     QARGRLRYDG TLGAFVPGEP VDGLTVIGSA AGEVVASKTL WRVPGPAEFQ FVDLQRDATV
     ADLRHAVGAG LRSIEHIKRF TTIGTAHDQG KTSGVLTTGI VAELLGVPVE AVGTTTFRPP
     YTPVAFAALA GRDRGHLFDP ERYTALHDWH VAAGAVFEDV GQWKRPRYYP RPGEDMPAAV
     LRECAAARTG VGLLDGSTLG KIDVRGPDAG VLLDRLYTNL MSSLKPGMVR YGVMCGVDGM
     VIDDGTVLRL ADDHFLVMTT TGGAAKILDW MEEWLQTEWP ELRVHLTSVT DHWATFPVVG
     PRSRDVVGAV FPDVDVSREA FPFLAIRETT LDGVPVRLAR ISFSGELAYE VYVSSWYAVA
     IWQRLLDAGR PHGLTPYGTE TMHVLRAEKG YPIIGQDTDG TVTPQDLGMA WVVSKKKADF
     VGKRSFARAA NLDPLRKHLV GLLPLDRRTV LPEGSQIVER LTEPPVAMLG HVTSSYRSAE
     LGRPFALALV KGGRERVGEV LQVPVDGTLV PVEVTGPVLV DPEGARRDG
//
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