ID R9C4E5_9BACI Unreviewed; 127 AA.
AC R9C4E5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
DE AltName: Full=Octanoyl/lipoyl carrier protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN ORFNames=A499_08909 {ECO:0000313|EMBL:EOR24172.1};
OS Niallia nealsonii AAU1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1202533 {ECO:0000313|EMBL:EOR24172.1, ECO:0000313|Proteomes:UP000014030};
RN [1] {ECO:0000313|EMBL:EOR24172.1, ECO:0000313|Proteomes:UP000014030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAU1 {ECO:0000313|EMBL:EOR24172.1,
RC ECO:0000313|Proteomes:UP000014030};
RA Joshi C.G., Duggirala S.M., Nathani N.M., Bhatt V.D., KaPatel J.A.,
RA Parnerkar S.P.;
RT "Whole genome shotgun sequencing of Bacillus nealsonii AAU1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Is also involved in protein lipoylation via its role as an
CC octanoyl/lipoyl carrier protein intermediate. {ECO:0000256|HAMAP-
CC Rule:MF_00272}.
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:EOR24172.1}.
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; ASRU01000095; EOR24172.1; -; Genomic_DNA.
DR RefSeq; WP_016202447.1; NZ_ASRU01000095.1.
DR AlphaFoldDB; R9C4E5; -.
DR PATRIC; fig|1202533.3.peg.1850; -.
DR OrthoDB; 9796712at2; -.
DR Proteomes; UP000014030; 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}.
FT DOMAIN 22..104
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 63
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 127 AA; 14224 MW; 16A53B9A924A4B28 CRC64;
MAVPKDLRYS KEHEWVKVEG ENARVGITYF AQSELGDIVF VELPEVGDEV TANEPFGSVE
SVKTVSELYA PISGKVVEVN EELSDNPEYV NESPYEKAWM VVIEPSDKAD IEALMSSEQY
EEMTNEG
//
