ID A0A1C3K2X2_9BURK Unreviewed; 951 AA.
AC A0A1C3K2X2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=ODI_01476 {ECO:0000313|EMBL:SBT25849.1}, ODI_R3789
GN {ECO:0000313|EMBL:SOE51924.1};
OS Orrella dioscoreae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Orrella.
OX NCBI_TaxID=1851544 {ECO:0000313|EMBL:SBT25849.1, ECO:0000313|Proteomes:UP000078558};
RN [1] {ECO:0000313|EMBL:SBT25849.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SBT25849.1};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SOE51924.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SOE51924.1};
RA de Groot N.N.;
RL Submitted (AUG-2017) 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; FLRC01000022; SBT25849.1; -; Genomic_DNA.
DR EMBL; LT907988; SOE51924.1; -; Genomic_DNA.
DR RefSeq; WP_067754527.1; NZ_LT907988.1.
DR AlphaFoldDB; A0A1C3K2X2; -.
DR STRING; 1851544.ODI_01476; -.
DR KEGG; odi:ODI_R3789; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000078558; Chromosome i.
DR Proteomes; UP000078558; 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; 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:UP000078558}.
FT DOMAIN 13..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 452..725
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 770..891
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 696
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 951 AA; 101352 MW; 7130E5EBD62D3C04 CRC64;
MPRVIDSDLD FTRRHIGPAS GDQQAMLAAV GAASLDALVA EVVPPAIRLD APLALPAGRS
EADVLDELRG LAERNEVFRS YIGQGYYGTH TPNVVLRNVL ENPAWYTAYT PYQPEISQGR
LEALLNFQTM VADLTALDIA NASLLDEGTA AAEAMALARR GARSKSPVFF VSRHCHPQTI
EVVRTRAEGL GIEIVEGDES QGLPECFGVL LQYPNSLGGV ADYRALAEQA HAQGAVVACA
TDLLALAVIA APGEWGADIA IGSAQRFGVP FGFGGPHAGF MACRDALKRS MPGRLVGVSR
DAQGRPALRL ALQTREQHIR REKATSNICT AQVLLAVMAG LYAVWHGPAG LAGIARRVHG
QAAALRAALV AAGHTVVNDT YFDTLCVETG ARTASVLEAA ASARINLRQV GATQVSLSLD
ETVTPADLAA LAEVFGASLG ELALADGLPG IPAGVARQSA ILSHPVFSSV QSETDMLRYL
RRLADKDLAL DRTMIPLGSC TMKLNATAEM LPITWPGFAH IHPFAPASQT RGYAELIERL
SAALCEITGY DAVSLQPNSG AQGEYAGLLA IRAYHRANGQ SQRDICLIPS SAHGTNPASA
QLVGMEVVVV ASDAQGNVDI EDLKRRIAQS GDRVAALMIT YPSTHGVFEE QVTQICELVH
EAGGQVYLDG ANMNAMVGIA KPGKFGSDVS HLNLHKTFCI PHGGGGPGVG PVAVRGHLAP
YLPGAVGSDG WLAEHTPVGP VSAAPFGSAG ILPIPYIYIL LMGAEGLKRA TEVAILNANY
IATRLKDHFP VLYSGRNGRV AHECILDVRE LKERTGISNE DIAKRLVDYG FHAPTMSFPV
PGTLMVEPTE SEGLLELDRF IDAMIAIREE IAQVERGERD REDNVLKNAP HTAQVLLADE
WHHAYPRQQA AYPLATLRDN KYWPPVSRVD NAYGDRNLVC ACLPMEAYAD A
//
