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Database: UniProt
Entry: A0A2E9CCM0_9ARCH
LinkDB: A0A2E9CCM0_9ARCH
Original site: A0A2E9CCM0_9ARCH 
ID   A0A2E9CCM0_9ARCH        Unreviewed;       138 AA.
AC   A0A2E9CCM0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Glycine cleavage system protein H {ECO:0000313|EMBL:MBS84938.1};
GN   ORFNames=CME83_00025 {ECO:0000313|EMBL:MBS84938.1};
OS   Candidatus Heimdallarchaeota archaeon.
OC   Archaea; Asgard group; Candidatus Heimdallarchaeota.
OX   NCBI_TaxID=2026747 {ECO:0000313|EMBL:MBS84938.1, ECO:0000313|Proteomes:UP000228988};
RN   [1] {ECO:0000313|Proteomes:UP000228988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GcvH family.
CC       {ECO:0000256|ARBA:ARBA00009249}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MBS84938.1}.
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DR   EMBL; PBWW01000001; MBS84938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2E9CCM0; -.
DR   Proteomes; UP000228988; Unassembled WGS sequence.
DR   GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:InterPro.
DR   CDD; cd06848; GCS_H; 1.
DR   Gene3D; 2.40.50.100; -; 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; IPR011053; Single_hybrid_motif.
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}.
FT   DOMAIN          31..113
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   138 AA;  15920 MW;  5176A0A480A96134 CRC64;
     MDFLKIGDYK IAKDRMYLSS HEWVLDNQDG TYTMGISDYA QKMLKEISYV QFEDEGDEFD
     KEDIVCVVEA LKATGDIYAP FDCELVANNE ELEDDPEIVS DSPYEGGWLV KIKKITDDND
     MISPEEYMKV IEAELNDF
//
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