GCSH_YEAST
ID GCSH_YEAST Reviewed; 170 AA.
AC P39726; D6VPH2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Glycine cleavage system H protein, mitochondrial;
DE AltName: Full=Glycine decarboxylase complex subunit H;
DE Flags: Precursor;
GN Name=GCV3; OrderedLocusNames=YAL044C; ORFNames=FUN40;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 14; 73 AND 90.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=9020168; DOI=10.1074/jbc.272.7.4444;
RA Nagarajan L., Storms R.K.;
RT "Molecular characterization of GCV3, the Saccharomyces cerevisiae gene
RT coding for the glycine cleavage system hydrogen carrier protein.";
RL J. Biol. Chem. 272:4444-4450(1997).
RN [4]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: The glycine cleavage system (glycine decarboxylase complex)
CC catalyzes the degradation of glycine. The H protein shuttles the
CC methylamine group of glycine from the P protein to the T protein (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:9020168}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC -!- SUBUNIT: Component of the glycine decarboxylase complex (GDC), which is
CC composed of four proteins: P, T, L and H.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}.
CC -!- INDUCTION: Induced by glycine and repressed by the C1 metabolic end
CC products. {ECO:0000269|PubMed:9020168}.
CC -!- MISCELLANEOUS: Present with 3510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC04987.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U12980; AAC04987.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006935; DAA06942.1; -; Genomic_DNA.
DR PIR; S51975; S51975.
DR RefSeq; NP_009355.3; NM_001178189.1.
DR AlphaFoldDB; P39726; -.
DR SMR; P39726; -.
DR BioGRID; 31783; 96.
DR ComplexPortal; CPX-1268; Glycine decarboxylase multienzyme complex.
DR IntAct; P39726; 1.
DR MINT; P39726; -.
DR STRING; 4932.YAL044C; -.
DR iPTMnet; P39726; -.
DR MaxQB; P39726; -.
DR PaxDb; P39726; -.
DR PRIDE; P39726; -.
DR EnsemblFungi; YAL044C_mRNA; YAL044C; YAL044C.
DR GeneID; 851254; -.
DR KEGG; sce:YAL044C; -.
DR SGD; S000000042; GCV3.
DR VEuPathDB; FungiDB:YAL044C; -.
DR eggNOG; KOG3373; Eukaryota.
DR GeneTree; ENSGT00390000011666; -.
DR HOGENOM; CLU_097408_2_0_1; -.
DR InParanoid; P39726; -.
DR OMA; YRDSHEW; -.
DR BioCyc; YEAST:G3O-28852-MON; -.
DR Reactome; R-SCE-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SCE-6783984; Glycine degradation.
DR ChiTaRS; GCV3; yeast.
DR PRO; PR:P39726; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39726; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0006546; P:glycine catabolic process; IMP:SGD.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IGI:SGD.
DR GO; GO:0009249; P:protein lipoylation; IMP:SGD.
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 1: Evidence at protein level;
KW Lipoyl; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 48..170
FT /note="Glycine cleavage system H protein, mitochondrial"
FT /id="PRO_0000010739"
FT DOMAIN 61..143
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 102
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 14
FT /note="T -> A (in Ref. 1; AAC04987)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="A -> S (in Ref. 1; AAC04987)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="A -> S (in Ref. 1; AAC04987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 170 AA; 18793 MW; 6DC35B6CCC71A6D6 CRC64;
MLRTTRLWTT RMPTVSKLFL RNSSGNALNK NKLPFLYSSQ GPQAVRYTSQ HEWIAVHQDK
TAFVGITKYA TDALGDATYV ELPEVGTEIA QGESLGSIES VKSASEIYQP ADGTVEEINT
NLEENPGVVN EDPMGDGWLV KMKLGEGVNV EQVEGLMSLE QYEKTLVHDD
