ID A0A0Q6UXN6_9ACTN Unreviewed; 958 AA.
AC A0A0Q6UXN6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=ASC64_09230 {ECO:0000313|EMBL:KQV69962.1};
OS Nocardioides sp. Root122.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736431 {ECO:0000313|EMBL:KQV69962.1, ECO:0000313|Proteomes:UP000051395};
RN [1] {ECO:0000313|EMBL:KQV69962.1, ECO:0000313|Proteomes:UP000051395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root122 {ECO:0000313|EMBL:KQV69962.1,
RC ECO:0000313|Proteomes:UP000051395};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV69962.1, ECO:0000313|Proteomes:UP000051395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root122 {ECO:0000313|EMBL:KQV69962.1,
RC ECO:0000313|Proteomes:UP000051395};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQV69962.1}.
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DR EMBL; LMDE01000010; KQV69962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q6UXN6; -.
DR STRING; 1736431.ASC64_09230; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000051395; 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:UP000051395}.
FT DOMAIN 25..448
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 449..733
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 779..900
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 706
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 958 AA; 101493 MW; A450E5F2ABD6A8D1 CRC64;
MPDVSPTSPT TSESTTSALG EFVPRHIGPD DAAVAHMLAA IGHESLESLM TAAVPGGIRT
AAALDLPDPL DEEATARALR TLASQNRPAE AMIGLGYHGT ITPPVIRRNV LEDPSWYTAY
TPYQPEISQG RLEALLNFQT VVADLTGLPT ANASLLDEGT AAAEAMTLVR RAQRNAAGPF
VIDADALPQT IDVVRTRAEG MGIEVVVADL RAGLPDGDLC GVLVQYPGAS GAVADPRAVI
DAAHERGALA VVAADLLALT LLEAPGTFGA DVVVGSSQRF GVPLFYGGPH AGFMSVSAGL
ERHLPGRLVG VSVDAEGRPA YRLALQTREQ HIRRDKATSN ICTAQVLLAV VASMYAVYHG
PEGLRRIAQR THDHASRIAA ALRAGGVQVV NDTWFDTLTV AVPGRAAEVI AAARAVGLHL
RLIDDDHVGL STSERTSAST VSAVLRSFGV AAAEGAPASG LPEELHRTTD YLTHEVFGSH
HSETQMLRYL HKLSGRDYAL DRGMIPLGSC TMKLNATTEM EPISLPGFAD LHPFAPAQDA
TGYRELVDDL EAWLAEVTGY DKVSVQPNAG SQGELAGLLA IRGYHRANGD LDRNICLIPS
SAHGTNAASA VMAGMKVVVV KASDDGSVDL DDLLAKCDQY ADTLAAIMVT YPSTHGAYED
TITDLCKVVH DHGGQVYVDG ANLNALLGYA RPGEFGGDVS HLNLHKTFCI PHGGGGPGVG
PVAVREHLAP YLPSHGWHPD AEKRSGIGPI SAAPYGSAGI LPITWAYIRM MGGAGLTRAT
AVAVLSANYI AHRLEEHFPV LYRGHGDLVA HECILDLRGL TKASGVSVDD VAKRLVDYGF
HAPTMSFPVA GTLMVEPTES EDLAEIDRFC DAMIAIRAEI ARVEAGEWTP EDSPLRHAPH
TARALVGEWD RGYTRELAVF PQGVDPDKYW PPVARIDQAY GDRNLVCACP PPEAFAQD
//
