GCSH_ORYSI
ID GCSH_ORYSI Reviewed; 164 AA.
AC A2Z9B8; O22535; Q0IWE1; Q7XCT9; Q94HZ9; Q9FW99;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Glycine cleavage system H protein, mitochondrial;
DE Flags: Precursor;
GN Name=GDCSH; ORFNames=OsI_033161;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Milyang 23; TISSUE=Seed;
RA Lee M.C., Kim C.S., Eun M.Y.;
RT "Isolation and characterization of H protein from rice.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The H protein shuttles the methylamine group of glycine from
CC the P protein to the T protein (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB82134.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB82134.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AF022731; AAB82134.1; ALT_SEQ; mRNA.
DR EMBL; CM000135; EAY79202.1; -; Genomic_DNA.
DR PIR; T02072; T02072.
DR AlphaFoldDB; A2Z9B8; -.
DR SMR; A2Z9B8; -.
DR STRING; 39946.A2Z9B8; -.
DR PRIDE; A2Z9B8; -.
DR EnsemblPlants; BGIOSGA033278-TA; BGIOSGA033278-PA; BGIOSGA033278.
DR Gramene; BGIOSGA033278-TA; BGIOSGA033278-PA; BGIOSGA033278.
DR HOGENOM; CLU_097408_1_0_1; -.
DR OMA; YRDSHEW; -.
DR Proteomes; UP000007015; Chromosome 10.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:InterPro.
DR CDD; cd06848; GCS_H; 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 PANTHER; PTHR11715; PTHR11715; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR00527; gcvH; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 2: Evidence at transcript level;
KW Lipoyl; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..164
FT /note="Glycine cleavage system H protein, mitochondrial"
FT /id="PRO_0000295027"
FT DOMAIN 56..138
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 97
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
SQ SEQUENCE 164 AA; 17367 MW; 9F6F9C3EF83E6312 CRC64;
MALRLWASSA ANALKISCSG ATRAAPAYSI SRYFSTVLDG LKYSSSHEWV KNDGSVATIG
ITDHAQGHLG EVVFVELPEA GAKVSQGGAF GNVESVKATS DINSPISGEV VEVNDKLSET
PGLINSSPYE DGWMIKVKPS SPSELDALLD PAKYTKHCEE EDAH
