ID A0A428NP53_9HYPO Unreviewed; 172 AA.
AC A0A428NP53;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
GN ORFNames=CEP53_012122 {ECO:0000313|EMBL:RSL42566.1};
OS Fusarium sp. AF-6.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL42566.1, ECO:0000313|Proteomes:UP000287544};
RN [1] {ECO:0000313|EMBL:RSL42566.1, ECO:0000313|Proteomes:UP000287544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL42566.1,
RC ECO:0000313|Proteomes:UP000287544};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:RSL42566.1}.
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DR EMBL; NKCJ01000405; RSL42566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428NP53; -.
DR STRING; 1325737.A0A428NP53; -.
DR Proteomes; UP000287544; 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; 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.
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:UP000287544};
KW Transit peptide {ECO:0000256|RuleBase:RU364055}.
FT DOMAIN 67..149
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 108
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 172 AA; 18420 MW; 67AD2B43F1FA1A1A CRC64;
MSGFIARQAW ATASRVRSSA LRAPQTVFAC KVASIAPRRC FSVSLNLLKR RYTESHEWID
LADDGKTCTI GISNYAAEAL GDVVYVELPA TGDETTEGES FGTVESVKSA SDIVAPVSGS
VIEVNEPLND TPADLGKDPE GEGWLIKVEA EDVSAIEGLM DEAAYAEHTK DH
//
