ID A0A0M2PRP1_PROHO Unreviewed; 970 AA.
AC A0A0M2PRP1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-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=PROH_15715 {ECO:0000313|EMBL:KKI99200.1};
OS Prochlorothrix hollandica PCC 9006 = CALU 1027.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Prochlorotrichales;
OC Prochlorotrichaceae; Prochlorothrix.
OX NCBI_TaxID=317619 {ECO:0000313|EMBL:KKI99200.1, ECO:0000313|Proteomes:UP000034681};
RN [1] {ECO:0000313|EMBL:KKI99200.1, ECO:0000313|Proteomes:UP000034681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CALU 1027 {ECO:0000313|EMBL:KKI99200.1};
RA Shanker A., Yadav P., Khan S., Sharma V.;
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKI99200.1, ECO:0000313|Proteomes:UP000034681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CALU 1027 {ECO:0000313|EMBL:KKI99200.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-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}.
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:KKI99200.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJTX02000006; KKI99200.1; -; Genomic_DNA.
DR RefSeq; WP_017712703.1; NZ_KB235937.1.
DR AlphaFoldDB; A0A0M2PRP1; -.
DR STRING; 317619.GCA_000332315_02309; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000034681; 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; 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:UP000034681}.
FT DOMAIN 25..447
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 486..743
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 789..910
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 714
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 970 AA; 104859 MW; BAC2F8914DFD6130 CRC64;
MTTFSPQPQS TQSPPALLEV KTFAQRHLGS GSDAIAQMLD QLGYKTLDAL VEMAVPQAIR
LQQPLPLGEG LSEAEALAQL KAIAQQNQVC HSYIGMGYAP CITPPVILRN ILENPGWYTA
YTPYQAEIAQ GRLEALLNFQ TLVTDLTGLA MANASLLDEA TAAAEAMALS YGAAKAKSQR
FFVSQDCHPQ TIEVVQTRAQ PLGIEVIVGD HQTFVPQAPI FGALLAYPAS DGTLYDYRPF
IAQVQQQGGL VTLVADLLSL VLLTPPGELG ADIAIGNTQR FGVPLGYGGP HAAYFATSTA
YQRKMPGRIV GLSKDANGNP ALRLALQTRE QHIRRDKATS NICTAQVLLA VIASMYGVYH
GPDGLKAIAH RVRQCTTALA AGLQHLGYDT DASHCFDTLK VVSDRAGSLW QAAADQGLNL
RYIDGQTLGI TLDETTTVAD LEQLLLCFAQ GGTLPVSLGD LLAQADVQVA PGFRRTSAFL
HQPVFNRYHS ETEMLRYLHR LEAKDLALNT SMIPLGSCTM KLNATAEMIP ITWPEFGQIH
PFAPLSQTQG YQVLFQQLEQ DLQDITGFAA VSLQPNAGSQ GEYAGLLVIR QYHQQRGDGH
RTVCLIPQSA HGTNPASAVM AGMTVVPVRC DDQGNVDLAD LTAKAQQHQE NLAALMVTYP
STHGVFEAEI RTICQIIHDH GGQVYMDGAN MNAQVGLCRP GDFGADVCHL NLHKTFCIPH
GGGGPGMGPI GVAAHLAPFL PGHGVLSNQN TLGSHPIGAV SAAPWGSASI LPISWMYIKM
MGAAGLTEAT QLAILNANYM AHRLAPHYPI LYKGIGGLVA HECILDLRDL KRTAGIEVED
VAKRLMDYGF HAPTVSWPVA GTMMVEPTES ESKEELDRFC DAMIAIRQEV RAIEQGQIDP
LNNPLKHAPH TAEVLLADDW DRPYSREQAA YPLPWLRQFK FWPVVGRVDN AYGDRNLVCS
CAPMEDYGTV
//
