ID A0A0J1CSD5_9BURK Unreviewed; 975 AA.
AC A0A0J1CSD5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=EOS_26620 {ECO:0000313|EMBL:KLU23201.1};
OS Caballeronia mineralivorans PML1(12).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU23201.1, ECO:0000313|Proteomes:UP000035963};
RN [1] {ECO:0000313|EMBL:KLU23201.1, ECO:0000313|Proteomes:UP000035963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX PubMed=26205858;
RA Uroz S., Oger P.;
RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT Ability.";
RL Genome Announc. 3:e00798-15(2015).
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:KLU23201.1}.
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DR EMBL; AEJF01000159; KLU23201.1; -; Genomic_DNA.
DR RefSeq; WP_047895179.1; NZ_AEJF01000159.1.
DR AlphaFoldDB; A0A0J1CSD5; -.
DR PATRIC; fig|908627.4.peg.5940; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000035963; 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}.
FT DOMAIN 28..454
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 466..762
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 795..916
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 722
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 975 AA; 104826 MW; C1888533F1BD95F7 CRC64;
MKLEHPDRLM NRSSLSLAAL ECHNAFAQRH IGPDAADQHA MLDALGFASR AAFIDAVIPE
SIRRHETLPL GAFTQPKSEA EALASLRKLA DQNLVFRNYI GQGYYGTHTP AVILRNVLEN
PAWYTAYTPY QPEISQGRLE ALLNFQQMVI DLTGLAISNA SLLDEATAAA EAMTLLQRAG
KPKSNLFYIA DDVLPQTIEV VQTRAKPAGI EVKVGPAADA ATANAFGVLL QYPGANGDVQ
DYRALAEAVH AAGGHVVVAA DLLALTLLTP PGEWGADVAI GNTQRFGVPV GFGGPHAAYM
AVRDDFKRQM PGRLVGVTID AQGKHALRLA LQTREQHIRR EKATSNVCTA QALLAIMASM
YAVYHGPQGL KTIALRVNRV ASIFAAGVQK LGYTLANETF FDTVTIVSGA NTTALHQAAS
AVHVNLRHID ATHVGISVDE TTTRDDLLKL FALFAEVLGK TETFDIDALD ADAKVSLPKA
LERTSEYLTH PVFNRHHSEH EMLRYLRSLA DKDLALDRTM IPLGSCTMKL NATSEMLPVT
WPEFAQIHPF APAEQTVGYR TMIDQLEQML VACTGYAAVS LQPNAGSQGE YAGLLIIHAY
HASRGEGHRN ICLIPSSAHG TNPASAQMAG MQVVVVACDE QGNVDIADLE AKAEKHAQNL
AAIMITYPST HGVFEANVRE ICEIVHGHGG QVYVDGANMN AMVGLTAPGQ FGGDVSHLNL
HKTFCIPHGG GGPGVGPVAV GAHLAKFLPN QHSTGYQRDA AGIGAVSSAP YGSAAILPIS
WMYIAMMGAQ GLTNATESAI LAANYVAKRL APHYPVLYSG TGGLVAHECI LDLRPLKETS
GISVDDVAKR LIDYGFHAPT MSFPVPGTLM VEPTESESKE ELDRFIDAMI AIRDEIRAVE
EGKSDREDNP LKHAPHTAAV VVADNWSHVY SRETAAYPLT SLIARKYWPP VGRADNAYGD
RNLFCSCIPL SEYGE
//
