ID B3QI71_RHOPT Unreviewed; 968 AA.
AC B3QI71;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 102.
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 OrderedLocusNames=Rpal_4375 {ECO:0000313|EMBL:ACF02871.1};
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=395960 {ECO:0000313|EMBL:ACF02871.1, ECO:0000313|Proteomes:UP000001725};
RN [1] {ECO:0000313|EMBL:ACF02871.1, ECO:0000313|Proteomes:UP000001725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1 {ECO:0000313|EMBL:ACF02871.1,
RC ECO:0000313|Proteomes:UP000001725};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-2008) 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; CP001096; ACF02871.1; -; Genomic_DNA.
DR RefSeq; WP_012497223.1; NC_011004.1.
DR AlphaFoldDB; B3QI71; -.
DR KEGG; rpt:Rpal_4375; -.
DR HOGENOM; CLU_004620_2_1_5; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000001725; 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; 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}.
FT DOMAIN 15..438
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 453..732
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 779..900
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 704
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 968 AA; 104091 MW; ECE85D02A9BB19B9 CRC64;
MPHRRPIDAA NDFVRRHIGP SPQDIAAMLA TAGAGSLEQL VAETLPYAIR HREPLKLGTP
LTESEALAHM SELGAQNQVF TSLIGQGYYG TILPTVIQRN ILENPAWYTA YTPYQPEISQ
GRLEALFNFQ TMICDLTGLD VANASLLDEG TAAAEAMALA ERAAAKNAKA FFVDADTHPQ
TIAVLRTRAE PLGWRIIVGN PETELEGADV FGALLQYPGS SGRLSDPRAV IAALRKKGAL
AVVAADLLAL TLITPPGELG ADIAIGSAQR FGVPMGYGGP HAAYMAVRDS LKRSLPGRIV
GLSIDSHGQP AYRLALQTRE QHIRREKATS NICTAQVLLA VINAMYAVYH GPDGLAAIAR
RVHRRTAVLA AGLQQLGFAP THSNYFDTLT IEVGDRRDAI VARAEAEKIN LRINASSLGI
SLDETTTPAT VEALWRAFGG SLDYAAVERD ASDALGSALP AALKRTSDYL TQPAFQDYRS
ETELLRYMRK LSDRDLALDR AMIPLGSCTM KLNATTEMMP LTWPEFGSLH PFVPKAQAAG
YHALFERLET WLAEITGYDA VSLQPNSGAQ GEYAGLLTIR GYHLSRGEPH RKVCLIPSSA
HGTNPASAAM AGMDVVVVAC DAHGDVDVDD LRAKAEAHSA NLAAVMITYP STHGVFEEHI
REICDIVHAH GGQVYLDGAN LNAQVGLARP GSYGADVSHL NLHKTFCIPH GGGGPGMGPI
GVKAHLAPFL PGHPAEGEPL NGGLHGGGTV SAAPWGSASI LTISYIYILM MGAAGLKRAT
EIAILNANYI AAKLHPHFPV LYRNPRGRVA HECIIDPRAL KTSTGVTVDD IAKRLIDYGF
HAPTMSFPVP GTLMIEPTES ESKAEIDRFC DAMIAIRREI AQVESGRYPI EQSPLRHAPH
TAHDVTSAEW TRPYPRTEGC FPAPNSRTDK YWSPVGRVDN VYGDRNLICS CPPVEDYALA
ADYARAAE
//
