ID H6BMB5_EXODN Unreviewed; 509 AA.
AC H6BMB5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Putative transferase CAF17, mitochondrial {ECO:0000256|ARBA:ARBA00018540};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395};
DE AltName: Full=Putative transferase caf17, mitochondrial {ECO:0000256|ARBA:ARBA00016916};
GN ORFNames=HMPREF1120_01197 {ECO:0000313|EMBL:EHY52996.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY52996.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY52996.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY52996.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + N(6)-[(R)-S(8)-
CC aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-
CC lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475,
CC Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00043710};
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH226130; EHY52996.1; -; Genomic_DNA.
DR RefSeq; XP_009153457.1; XM_009155209.1.
DR AlphaFoldDB; H6BMB5; -.
DR STRING; 858893.H6BMB5; -.
DR GeneID; 20305836; -.
DR VEuPathDB; FungiDB:HMPREF1120_01197; -.
DR eggNOG; KOG2770; Eukaryota.
DR HOGENOM; CLU_007884_10_0_1; -.
DR InParanoid; H6BMB5; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 5473523at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; 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; 4.10.1250.10; Aminomethyltransferase fragment; 1.
DR InterPro; IPR006223; GCS_T.
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 NCBIfam; TIGR00528; gcvT; 1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR PIRSF; PIRSF006487; GcvT; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Methyltransferase {ECO:0000313|EMBL:EHY52996.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EHY52996.1}.
FT DOMAIN 105..386
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 420..500
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 509 AA; 56090 MW; 0FD57F0E36018699 CRC64;
MSPYRGLRPL LAASSGAGRP IRWMPRRELS SLNSASSFIP SLSTCQRQDA SPPYHWKTPP
ALSLVRSTTL QQWTSRSRFV TKFAQRHSYS TSSESGEQEL KRTPLYELHT SLGAKMVPFA
EFAMPLEYPD QSHRESHLWT RSNASLFDVS HMVQHKMSGE LAEEFLMTIT PSAINEIEKH
HSTLSCLLNK QGGIVDDTVI TRIGKDSFYF VTNAGCRKGD LAFIEAEMDE FLKSKGNPKD
KAINWHVLDH HALIALQGPA AASVLQSLVY NDTEDESYDT KLDSLYFGTS RWLQLTLPET
GMNTPSLLIT RTGYTGEDGF EISIPPENGD ATELATSIAK ALTADSSKVR WAGLGARDSL
RLEAGMCLYG HDLNDTITPP VASLGWLVGK SRRGENPQPP FNGHEIINKQ LASPKTMPQR
RVGFLVEKGP AAREGAEIVD PGSDNQVIGH VTSGCPSPSL GGQNIAMGYV KNGFHKKGTK
VGIKVRKNVR QAEVAKMPFV ESKFYRPST
//
