ID A0A246K3H5_9SPHN Unreviewed; 123 AA.
AC A0A246K3H5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272,
GN ECO:0000313|EMBL:OWR00111.1};
GN ORFNames=CDQ91_04880 {ECO:0000313|EMBL:OWR00111.1};
OS Sphingopyxis witflariensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=173675 {ECO:0000313|EMBL:OWR00111.1, ECO:0000313|Proteomes:UP000197097};
RN [1] {ECO:0000313|EMBL:OWR00111.1, ECO:0000313|Proteomes:UP000197097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14551 {ECO:0000313|EMBL:OWR00111.1,
RC ECO:0000313|Proteomes:UP000197097};
RX PubMed=12508864; DOI=10.1099/ijs.0.02217-0;
RA Kampfer P., Witzenberger R., Denner E.B., Busse H.J., Neef A.;
RT "Sphingopyxis witflariensis sp. nov., isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 52:2029-2034(2002).
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. {ECO:0000256|HAMAP-Rule:MF_00272}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00272};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000256|HAMAP-
CC Rule:MF_00272};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|HAMAP-Rule:MF_00272}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|ARBA:ARBA00009249,
CC ECO:0000256|HAMAP-Rule:MF_00272}.
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:OWR00111.1}.
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DR EMBL; NISJ01000002; OWR00111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246K3H5; -.
DR OrthoDB; 9796712at2; -.
DR Proteomes; UP000197097; 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: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:SF41; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 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|HAMAP-Rule:MF_00272};
KW Reference proteome {ECO:0000313|Proteomes:UP000197097}.
FT DOMAIN 18..100
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 59
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 123 AA; 13125 MW; 1059D540F30287FB CRC64;
MPRYYTEEHE WLDVDGDVAT VGITDFAQGQ LGDIVFVEVP DTGAELTAGG DAAVVESVKA
ASDVYAPVDG TVTEGNGQLE EDPALVNSDP EGEGWFFRMT LSDKSQLDAL MNAAAYKAFC
DDL
//