ID A0A1Y1HQE8_KLENI Unreviewed; 162 AA.
AC A0A1Y1HQE8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 08-NOV-2023, entry version 22.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
GN ORFNames=KFL_000640220 {ECO:0000313|EMBL:GAQ80855.1};
OS Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ80855.1, ECO:0000313|Proteomes:UP000054558};
RN [1] {ECO:0000313|EMBL:GAQ80855.1, ECO:0000313|Proteomes:UP000054558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ80855.1,
RC ECO:0000313|Proteomes:UP000054558};
RX PubMed=24865297; DOI=10.1038/ncomms4978;
RA Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA Tabata S., Ida S., Kurokawa K., Ohta H.;
RT "Klebsormidium flaccidum genome reveals primary factors for plant
RT terrestrial adaptation.";
RL Nat. Commun. 5:3978-3978(2014).
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; DF237013; GAQ80855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1HQE8; -.
DR STRING; 105231.A0A1Y1HQE8; -.
DR OrthoDB; 52189at2759; -.
DR Proteomes; UP000054558; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
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|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU364055};
KW Reference proteome {ECO:0000313|Proteomes:UP000054558};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU364055}.
FT DOMAIN 55..137
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 96
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 162 AA; 17411 MW; 5BD8ABCC5AAA5CF7 CRC64;
MALKMVATEL VGALRMRCQP GAASSLLFFL RPFSTAPQGT KYLTSHEWVN VQDGVGTVGI
SDFAQNELGD VVFVELPEVG ATVTKGETFG VVESVKAASD VYSPVTGEVV ERNDSLTETP
ALVNKGPFDD GWMLKVKLSN PSDVEDLLDA SAYEKHCEDS TH
//
