ID A0A0C1KZF6_9BACT Unreviewed; 956 AA.
AC A0A0C1KZF6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711};
GN ORFNames=OI18_19220 {ECO:0000313|EMBL:KIC93072.1};
OS Flavihumibacter solisilvae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1349421 {ECO:0000313|EMBL:KIC93072.1, ECO:0000313|Proteomes:UP000031408};
RN [1] {ECO:0000313|EMBL:KIC93072.1, ECO:0000313|Proteomes:UP000031408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-3 {ECO:0000313|EMBL:KIC93072.1,
RC ECO:0000313|Proteomes:UP000031408};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter solisilvae 3-3.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein binds the alpha-amino group of glycine through
CC its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC methylamine moiety is then transferred to the lipoamide cofactor of the
CC H protein. {ECO:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83143; EC=1.4.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
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:KIC93072.1}.
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DR EMBL; JSVC01000023; KIC93072.1; -; Genomic_DNA.
DR RefSeq; WP_039142781.1; NZ_JSVC01000023.1.
DR AlphaFoldDB; A0A0C1KZF6; -.
DR STRING; 1349421.OI18_19220; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000031408; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR003437; GcvP.
DR InterPro; IPR049316; GDC-P_C.
DR InterPro; IPR049315; GDC-P_N.
DR InterPro; IPR020581; GDC_P.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00461; gcvP; 1.
DR PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR Pfam; PF02347; GDC-P; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000031408}.
FT DOMAIN 14..438
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 459..734
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 773..894
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 705
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 956 AA; 104416 MW; B9073FDCB6989891 CRC64;
MNLFQSQSNE FPARHIGTLS STKELLAVTG YKRLEELIDR TIPASIRKKD ELSVPDAVSE
AQLLKELKEI SLKNKVFRNY IGQGYYDTIT PSVILRNIFE NPGWYTQYTP YQAEISQGRL
ESLLNYQTMI SDLTGLPLAN ASLLDEATAA AEAMNMFFHH VNRTEQINQP RFFVDNNVFR
QTKDLLITRA NPIGIEVVFG DYRNAAIDNS YFGALIQYPG EDGSIEDFRS FINTIHSVGG
YVAMATDLLA LTLLTPPGEL GADVAFGSAQ RFGVPLGYGG PHAAFFSAKD DFKRSIPGRI
IGVSVDAAGN RALRMALQTR EQHIKREKAT SNICTAQALL ANMAAMYAVY HGPAGLRNIA
KRTALLTRTL AIELGNLGFE VINQNFFDTI HVSTNNVDAV RENALNQQIN FYYSENTIGI
SLDETTTQSD VLDIVSVFAA SIGEDTSSVI FDNEASLDNI PSSLTRTSLY LTHPVFNSHR
SESQMMRYIK SLENKDLSLN TSMISLGSCT MKLNAATEMI PLSWSHFSRI HPFAPVDQAA
GYQQVISELS AFLCNITGLD ACSMQPNSGA QGEYAGLLAI RNYHIATGHG HRNVILIPIS
AHGTNPASAV MAGMKVVVVK ALENGYIDVD DFKAKAEQHS ANLAGTMITY PSTYGIFEEG
VKDICDVVHQ HGGQVYLDGA NMNAQVGLTS PGLIGADVCH LNLHKTFAIP HGGGGPGMGP
ICVKSHLAPH LPGHWSLGDG KSAVSAAPYG SASILLISYA YCRMLGASGL KASTEYAILN
ANYMKARLES AYPILYTSHN GTCAHEFIVD LRPFKTSAGI EAEDIAKRLM DYGFHAPTMS
FPVPGTIMIE PTESEDKAEL DRFCDALLAI REEIAAVENG TADKTNNVLK NAPHTQFVIT
ADEWQRPYSR QQAAFPLDYV KENKFWPSVG RVNNTVGDRN LICTCEPVSA YEEAVS
//
