ID A0A076H6M3_9SYNE Unreviewed; 960 AA.
AC A0A076H6M3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=KR49_08185 {ECO:0000313|EMBL:AII44808.1};
OS Synechococcus sp. KORDI-49.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=585423 {ECO:0000313|EMBL:AII44808.1, ECO:0000313|Proteomes:UP000028589};
RN [1] {ECO:0000313|EMBL:AII44808.1, ECO:0000313|Proteomes:UP000028589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI-49 {ECO:0000313|EMBL:AII44808.1,
RC ECO:0000313|Proteomes:UP000028589};
RA Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT "Genome sequences of Synechococcus sp. KORDI-49.";
RL Submitted (JUN-2013) 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; CP006270; AII44808.1; -; Genomic_DNA.
DR RefSeq; WP_043693571.1; NZ_CP006270.1.
DR AlphaFoldDB; A0A076H6M3; -.
DR STRING; 585423.KR49_08185; -.
DR KEGG; synr:KR49_08185; -.
DR PATRIC; fig|585423.3.peg.1563; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_2_1_3; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000028589; 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 7..437
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 629..732
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 775..896
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 960 AA; 103357 MW; C36AB5DDBA4B9EA6 CRC64;
MVSPFLERHL GPGNAEQRSM LKTLGYSDMA AFIADVVPSD ILDEHPPSEA MPEGCSESEA
LEDLRRIVAD NTVRRSLIGL GYHGTATPAL IQRHVFENPA WYTAYTPYQA EIAQGRLEAL
LNFQTLISEL TGLPIANASL LDEATAAAEA MGLSHAVCRR AEARRFLVDA AVLPQTWAVL
QTRAEPLNIE LERLDPGDFV LDATVFGVLL QLPGKEGQVW DPTALIERAH EAGALVTVAI
DPLAQTLIAP VASFGADIAV GSAQRFGVPM GFGGPHAAFF ATRDAYKRQI PGRLVGQSRD
AQGQPALRLA LQTREQHIRR DKATSNICTA QVLLAVMASF YAVHHGPDGL TAIAQRIVRL
RRRLEAALVA LGYPVAPGER FDTVVIRCSD AAAVHRAAAE AEINLRVVPE GAAPDQAEGF
GITLDELSNE SELKRLVLLL AAAAQRQTPP ITEVVSGSLD GVPGREEPWL TQAVFHCHRS
ETELLRYIQR LVSRDLSLVH GMIPLGSCTM KLNAAAELLP VSWPAFASLH PFAPEDQARG
YRHMADDLER WLAALTGFSA VSLQPNAGSQ GEYAGLLVIR AWHHSRGDSH RDICLIPTSA
HGTNPASAVM AGLKVVPVAC DDEGNVDLDD LAARAEEFSD RLAALMVTYP STHGVFEPGI
RQICSVVHRH GGQVYLDGAN LNAQVGLCRP GAFGADVCHL NLHKTFCIPH GGGGPGVGPI
GVAEHLAPFL PGHPLQSDQP TAIGPVSAAP LGSASILPIS WMYLRMMGAE ALRQASAVAL
LSANYLAHRL DPHYPVLFRG TTGCVAHECI LDLRPLKRDA GVDVDDIAKR LMDYGFHAPT
VSWPVAGTVM VEPTESESLE ELDRFADALI AIREEVRDIE SGRMDPVNNP LKRAPHTMAV
VTADVWDRPY SRATAAFPLA DQPMNKLWPA VGRIDNAFGD RNLICTCPSV EDLAEQPVAA
//
