ID W6ZIX8_COCMI Unreviewed; 169 AA.
AC W6ZIX8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
GN ORFNames=COCMIDRAFT_22528 {ECO:0000313|EMBL:EUC49975.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC49975.1};
RN [1] {ECO:0000313|EMBL:EUC49975.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC49975.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(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; KI963927; EUC49975.1; -; Genomic_DNA.
DR RefSeq; XP_007683519.1; XM_007685329.1.
DR AlphaFoldDB; W6ZIX8; -.
DR STRING; 930090.W6ZIX8; -.
DR GeneID; 19120268; -.
DR KEGG; bor:COCMIDRAFT_22528; -.
DR eggNOG; KOG3373; Eukaryota.
DR HOGENOM; CLU_097408_1_2_1; -.
DR OrthoDB; 52189at2759; -.
DR Proteomes; UP000054032; 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 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 169 AA; 18137 MW; 86F52154F2DEA53C CRC64;
MAARLSIALA ARRISSVAAR RPSLIVSQKW QQVAPKQRLF SVSAALKEKR YTEDHEWIEL
SADGKTCTLG ISEYAAKALG DVVYIELPQV DMEVAEGDVI GAVESVKSAS DILTPIAGVV
SEVNEALETA PGSVNKDPEG DAWVAKIAVS AEPKGKTMSK EEYATFTEE
//
