ID A0A0Q0AV93_PSESX Unreviewed; 127 AA.
AC A0A0Q0AV93;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN ORFNames=ALO94_01091 {ECO:0000313|EMBL:KPY79054.1}, ALP50_03768
GN {ECO:0000313|EMBL:RMT38183.1};
OS Pseudomonas syringae pv. spinaceae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=264459 {ECO:0000313|EMBL:KPY79054.1, ECO:0000313|Proteomes:UP000050384};
RN [1] {ECO:0000313|EMBL:KPY79054.1, ECO:0000313|Proteomes:UP000050384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP16929 {ECO:0000313|EMBL:KPY79054.1,
RC ECO:0000313|Proteomes:UP000050384};
RA Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.;
RT "Genome announcement of multiple Pseudomonas syringae strains.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RMT38183.1, ECO:0000313|Proteomes:UP000280047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 16928 {ECO:0000313|EMBL:RMT38183.1,
RC ECO:0000313|Proteomes:UP000280047};
RA Dillon M., Thakur S., Almeida R.N.D., Weir B.S., Guttman D.S.;
RT "Recombination of ecologically and evolutionarily significant loci
RT maintains genetic cohesion in the Pseudomonas syringae species complex.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:KPY79054.1}.
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DR EMBL; LJRI01001024; KPY79054.1; -; Genomic_DNA.
DR EMBL; RBTF01000007; RMT38183.1; -; Genomic_DNA.
DR RefSeq; WP_007244906.1; NZ_RBTF01000007.1.
DR AlphaFoldDB; A0A0Q0AV93; -.
DR PATRIC; fig|264459.3.peg.1964; -.
DR Proteomes; UP000050384; Unassembled WGS sequence.
DR Proteomes; UP000280047; 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; 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.
PE 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|HAMAP-Rule:MF_00272}.
FT DOMAIN 20..101
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 60
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 127 AA; 13842 MW; 33DE65A4D5638DFE CRC64;
MSELRFTVDH EWLRAEADGS VTVGITPYAQ ESLGDVVFVQ LPELQAYAQH AEVSVVESVK
AASSINMPLD GEVVEVNAVL DATPERVNED ALGAGWFFRF IPQDADAIHG LLDQDAYDRL
IKANAQA
//
