ID A0A1I7KJZ2_9BURK Unreviewed; 964 AA.
AC A0A1I7KJZ2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN04489707_10555 {ECO:0000313|EMBL:SFU97778.1};
OS Paenacidovorax caeni.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paenacidovorax.
OX NCBI_TaxID=343013 {ECO:0000313|EMBL:SFU97778.1, ECO:0000313|Proteomes:UP000183656};
RN [1] {ECO:0000313|EMBL:SFU97778.1, ECO:0000313|Proteomes:UP000183656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-24608 {ECO:0000313|EMBL:SFU97778.1,
RC ECO:0000313|Proteomes:UP000183656};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FPBX01000055; SFU97778.1; -; Genomic_DNA.
DR RefSeq; WP_054257496.1; NZ_FPBX01000055.1.
DR AlphaFoldDB; A0A1I7KJZ2; -.
DR STRING; 343013.SAMN04489707_10555; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000183656; 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; 1.
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:UP000183656}.
FT DOMAIN 21..450
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 460..744
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 785..906
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 715
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 964 AA; 102868 MW; A8F724F00ACBFEB2 CRC64;
MNAPAAPSLS ALENAAEFQP RHIGIDAFDE AHMLSVIGEA SRRALIDSIV PRSIARSRGM
DLPAPVTEAA ALAELKAIAS QNRLLKNFIG QGYYGTHTPG VILRNILENP AWYTAYTPYQ
AEISQGRMEA LVNFQTMVCD LTAMPIANAS MLDEATAAAE AMTLAKRSVK AKGNVFIVSG
DCHPQTIEVI QTRAAPLGIS VKVIRSGDEW LAAIAQDDYF AALNQYPGSS GWLADWQQSA
DLIHTKGAAF ILAADLLALT LLKAPGEMGA DIVVGTTQRF GMPMGAGGPH AAFMACRDDY
KRSLPGRLVG VSVDVHGQPA YRLALQTREQ HIRREKATSN ICTAQVLPAV IASMYAVYHG
PQGLTRIAQR VARLTAILAA GLKQLGLAPL HASAFDTLTV DLGSAAAAQA VLQRAQDAGI
NLRSLRGQCV GVSLDETTTR ADLALLWQAF APQAAQPSVE QLEASAASLI PASLARTSSF
LTHPVFNTHH SETGMLRYIR ALSDKDLALD RSMIPLGSCT MKLNATSEMI PITWPEFANV
HPFAPAEQLQ GYRQLDEQLR AWLCQATGYA GVSLQPNAGS QGEYAGLLAI KAYHAAQGQG
HRTVCLIPSS AHGTNPASAQ MVGMQVVVTK CDENGNVDMQ DLQAKCEQHS QNLACVMITY
PSTHGVFETQ VKELCELVHR HGGRVYVDGA NMNALVGVAA PGEFGGDVSH LNLHKTFCIP
HGGGGPGVGP VCVVADLVPY LPGHATAGVT GGTGAVSAAP LGNAAVLPIS WMYIRMMGAE
GLTAATEAAI LSANYISARL KDHYPTLYAS ANGHVAHECI LDLRGLKESS GVMAEDVAKR
LIDYGFHAPT LSFPVANTLM VEPTESETLA ELDRFIDAMI AIREEVRQVE NGTWPQDDNP
LKNAPHTAPS LLTGDWAHPY TRETAAYPVA SLRHTKYWSP VGRVDNVYGD RNLFCSCVPV
SELA
//
