ID I3YJY0_ALIFI Unreviewed; 125 AA.
AC I3YJY0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN OrderedLocusNames=Alfi_0935 {ECO:0000313|EMBL:AFL77298.1};
OS Alistipes finegoldii (strain DSM 17242 / JCM 16770 / CCUG 46020 / CIP
OS 107999 / KCTC 15236 / AHN 2437).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=679935 {ECO:0000313|EMBL:AFL77298.1, ECO:0000313|Proteomes:UP000006052};
RN [1] {ECO:0000313|Proteomes:UP000006052}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 17242 / JCM 16770 / AHN 2437 / CCUG 46020 / CIP 107999
RC {ECO:0000313|Proteomes:UP000006052};
RX PubMed=23961309; DOI=10.4056/sigs.3527032;
RA Mavromatis K., Stackebrandt E., Munk C., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Rohde M., Gronow S., Goker M.,
RA Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the bile-resistant pigment-producing anaerobe
RT Alistipes finegoldii type strain (AHN2437(T)).";
RL Stand. Genomic Sci. 8:26-36(2013).
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}.
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DR EMBL; CP003274; AFL77298.1; -; Genomic_DNA.
DR RefSeq; WP_009598413.1; NC_018011.1.
DR AlphaFoldDB; I3YJY0; -.
DR STRING; 679935.Alfi_0935; -.
DR GeneID; 79836261; -.
DR KEGG; afd:Alfi_0935; -.
DR PATRIC; fig|679935.3.peg.864; -.
DR eggNOG; COG0509; Bacteria.
DR HOGENOM; CLU_097408_2_2_10; -.
DR Proteomes; UP000006052; Chromosome.
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 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 125 AA; 13326 MW; 283CCB3EC5FF19DD CRC64;
MNVPANLKYS NDHEWCRIEG DTAVIGITDF AQSQLGDIVF VDVPTVGETL AAGEVFGSIE
AVKTVSDAFL PVGGEIVEFN DAVDADPAIV NKDAYGEGWI VKVKMSDPAE YDALLSAADY
EKLIG
//
