ID A0A0P0CRZ9_9BACT Unreviewed; 972 AA.
AC A0A0P0CRZ9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=DC20_09890 {ECO:0000313|EMBL:ALI99230.1};
OS Rufibacter tibetensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=512763 {ECO:0000313|EMBL:ALI99230.1, ECO:0000313|Proteomes:UP000061382};
RN [1] {ECO:0000313|EMBL:ALI99230.1, ECO:0000313|Proteomes:UP000061382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1351 {ECO:0000313|EMBL:ALI99230.1,
RC ECO:0000313|Proteomes:UP000061382};
RA Dai J.;
RT "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT radiation-resistant bacterium from tibet plateau.";
RL Submitted (AUG-2015) 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}.
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DR EMBL; CP012643; ALI99230.1; -; Genomic_DNA.
DR RefSeq; WP_062543687.1; NZ_CP012643.1.
DR AlphaFoldDB; A0A0P0CRZ9; -.
DR STRING; 512763.DC20_09890; -.
DR KEGG; rti:DC20_09890; -.
DR PATRIC; fig|512763.3.peg.2181; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000061382; Chromosome.
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; 1.
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:UP000061382}.
FT DOMAIN 13..444
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 484..744
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 785..905
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 713
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 972 AA; 107304 MW; 15FB9ABD3881C888 CRC64;
MIFKTKPADI FKERHNGPVK EQMQDMLQTI GAASLDQLID ETVPPAIRLK RPLNLPAPLT
ERDFLRKFAK IAKQNKLYKS YIGLGYHDTI LPPVIQRNIL ENPGWYTAYT PYQAEIAQGR
LEALINYQTL IIDLTGMAIA NASLLDEATA AAEAMNLQYS LRKGARKNAN RYFVSDQVLP
QTIDVLLSRA TPLGIELVLG DHRELNLQDD TLFGALVQYP AADGEVFDYT DFIAQAHEAS
VPVAVAADLL SLTLLKSPGE MGADVVVGSS QRFGVPMGYG GPHAGFFATK DEYKRSIPGR
IIGLSQDAFG QKAYRMALQT REQHIRREKA TSNICTAQVL LAVMAGMYAV YHGPRRLKYI
GLNIHSLTQI LEKGLERLGF EQLNENYFDT LNLRIESAEL QQAIRQEAEA TQINFRYFGD
NNNIGISLNQ NTDLDEVKDI LAVFAKVAGK PDATLELDAI PEETDITWPE ALIRTSPYLQ
AEVFNKYHSE SEILRYMKYL ENKDFSLAHG MIPLGSCTMK LNATAEMIPV TWPEIGQMHP
FAPADQAQGY AQIFQDLETW LCEVTGFAAM SLQPNSGAQG EYAGLMVIRA YHEACGDHHR
NISLIPSSAH GTNPASAVMA GMKVVIVKCD ERGNIDVADL RAKAEEHKDD LSCLMVTYPS
THGVYEESII EICEIIHQNG GRVYMDGANM NAQVGLTSPA NIGADVCHLN LHKTFCIPHG
GGGPGVGPIG VVADLAPFLP GHAVVDLERP EAINAVSAAP WGSASILPIS YAYINMMGGE
GLTEATKMAI LNANYIKARL EEHYPVLYVG SNGRCAHEMI LDCRSFKKAG VEVEDIAKRL
MDYGFHAPTV SFPVAGTLMV EPTESESKEE LDRFCDAMIS IREEIREVEE GKADQKNNLL
KNAPHPAHVA LAENWTFPYT RERAVYPVPY TRTAKFWPTV SRIDSAYGDR NLVCSCAPIE
AYNEQGQEMK AI
//
