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Database: UniProt
Entry: B6GX77_PENRW
LinkDB: B6GX77_PENRW
Original site: B6GX77_PENRW 
ID   B6GX77_PENRW            Unreviewed;       170 AA.
AC   B6GX77;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
GN   ORFNames=Pc12g15080 {ECO:0000313|EMBL:CAP81135.1}, PCH_Pc12g15080
GN   {ECO:0000313|EMBL:CAP81135.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP81135.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP81135.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; AM920427; CAP81135.1; -; Genomic_DNA.
DR   RefSeq; XP_002558311.1; XM_002558265.1.
DR   AlphaFoldDB; B6GX77; -.
DR   STRING; 500485.B6GX77; -.
DR   GeneID; 8308163; -.
DR   KEGG; pcs:Pc12g15080; -.
DR   VEuPathDB; FungiDB:PCH_Pc12g15080; -.
DR   eggNOG; KOG3373; Eukaryota.
DR   HOGENOM; CLU_097408_1_2_1; -.
DR   OMA; PYGKGWM; -.
DR   OrthoDB; 52189at2759; -.
DR   BioCyc; PCHR:PC12G15080-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c12.
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:UP000000724};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU364055}.
FT   DOMAIN          66..148
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         107
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
SQ   SEQUENCE   170 AA;  18113 MW;  083E1B70283DB927 CRC64;
     MSSVARAIRP FASRVLSQKP LASACQVSPA FRFPRGTRSF SQSPLSQLKK YTESHEWIEL
     ADGGKTAKIG ITEYAAHSLG DVVFVELPEV DLEIVAGEPV GAVESVKSAS DVLSPVAGKV
     IKGNSILEDK AKTINESPEG EGWIAEIEVA DVAELDALLD EAAYKETIDA
//
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