ID M7TQX0_EUTLA Unreviewed; 176 AA.
AC M7TQX0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
GN ORFNames=UCREL1_3894 {ECO:0000313|EMBL:EMR69085.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR69085.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- FUNCTION: The H protein shuttles the methylamine group of glycine from
CC the P protein to the T protein. {ECO:0000256|RuleBase:RU364055}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU364055};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000256|RuleBase:RU364055};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|RuleBase:RU364055}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU364055}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|ARBA:ARBA00009249,
CC ECO:0000256|RuleBase:RU364055}.
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DR EMBL; KB706136; EMR69085.1; -; Genomic_DNA.
DR RefSeq; XP_007791820.1; XM_007793629.1.
DR AlphaFoldDB; M7TQX0; -.
DR STRING; 1287681.M7TQX0; -.
DR KEGG; ela:UCREL1_3894; -.
DR eggNOG; KOG3373; Eukaryota.
DR HOGENOM; CLU_097408_1_2_1; -.
DR OMA; PYGKGWM; -.
DR OrthoDB; 52189at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR CDD; cd06848; GCS_H; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR HAMAP; MF_00272; GcvH; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR002930; GCV_H.
DR InterPro; IPR033753; GCV_H/Fam206.
DR InterPro; IPR017453; GCV_H_sub.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR00527; gcvH; 1.
DR PANTHER; PTHR11715; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 1.
DR PANTHER; PTHR11715:SF3; GLYCINE CLEAVAGE SYSTEM H PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|PIRSR:PIRSR617453-50};
KW Mitochondrion {ECO:0000256|RuleBase:RU364055};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU364055}.
FT DOMAIN 64..150
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 105
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 176 AA; 19115 MW; 51A5E03CDFA4E611 CRC64;
MASIARCLRA TRPTSAFSRL VQTPCVRANW QASTIRAFSA SPIREIRKYT KDHEWIDLNA
DKTTGVIGIS EYAAEELGDV VYVELPEEGK EVGRGDAIGA VESVKSAADI NAPVTCKITH
VNLVLEEKPG TINQVPEDDS HGGGWIAKVE VGEAAAQELE ALMDAEEYKT YTTAEH
//
