ID A0A0A1GYY9_9BURK Unreviewed; 950 AA.
AC A0A0A1GYY9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=E1O_01220 {ECO:0000313|EMBL:BAP87253.1};
OS Burkholderiales bacterium GJ-E10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1469502 {ECO:0000313|EMBL:BAP87253.1, ECO:0000313|Proteomes:UP000031649};
RN [1] {ECO:0000313|EMBL:BAP87253.1, ECO:0000313|Proteomes:UP000031649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GJ-E10 {ECO:0000313|EMBL:BAP87253.1,
RC ECO:0000313|Proteomes:UP000031649};
RA Fukushima J., Tojo F., Asano R., Kobayashi Y., Shimura Y., Okano K.,
RA Miyata N.;
RT "Complete Genome Sequence of the Unclassified Iron-Oxidizing,
RT Chemolithoautotrophic Burkholderiales bacterium GJ-E10 Isolated from Acid
RT River.";
RL Submitted (NOV-2014) 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; AP014683; BAP87253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1GYY9; -.
DR STRING; 1469502.E1O_01220; -.
DR KEGG; bbag:E1O_01220; -.
DR HOGENOM; CLU_004620_3_2_4; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000031649; 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; 1.
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:UP000031649}.
FT DOMAIN 18..438
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 455..729
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 702
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 950 AA; 101713 MW; 0BE4AECC74A3F2AF CRC64;
MYDGLQTPDR EGSGDFIDRH IGPDGEEIAG MLAELGVASL DDLSDAIVPP AIRLREPLAL
GAPASEAQAL RRMAEFAQRN QVARSLIGMG YHGTVMPPVI ARNVFENPAW YTAYTPYQAE
ISQGRLEAML NFQTLVADLT GLPIANASLL DEATAAAEAM MLARRSARSK SHRFFVAADC
HPQTIAVLHT RAEPLGIELV VGDDPLAAGE CFGALLQFPA STGKLRDHGA VAAALHARGA
LLAVATDLLA LTLLVPPGRW GADIAVGSAQ RFGVPMGFGG PHAGFLSCRD ELKRSMPGRI
VGISVDSQGK RALRLALQTR EQHIRREKAT SNICTAQVLL AVLASMYAVY HGPEGLRRIA
LRTHRLAAIF AAGLRAGGTT VSEAFFDTVR VDGVDARAVL AAAVARGYNL RGIAADAVGV
SFDETCGRED VVALWDAFGV RADFDALDRA HDDFARIPAA LRREADYLAH PVFHRHRSET
AMLRYLRGLA DRDLALDRTM IPLGSCTMKL NATSELLPVS WPQFANVHPF APADQTEGYR
EMIASLEAML AACTGYDRVS LQPNSGAQGE FAGLLAIRAY HRAQGQAQRT VCLIPESAHG
TNPASAAMAG MEVVVVDCDA NGNIDVTDLA TKAQLHAGRL AALMVTYPST HGVFEESIRE
VCDIVHRHGG QVYLDGANLN ALVGLAKPAE IGSDVSHLNL HKTFAIPHGG GGPGVGPVAV
RAHLAPYLPR TGDGAGTVGP VSAAPFGSAS ILPISWMYCA MMGAAGLTRA TQVALLNANY
LARKLAPHYP VLYTGRNGYV AHECILDLRP IKDRCGITAE DVAKRLMDYG FHAPTLSFPV
PGTLMVEPTE SESRAELDRF VEAMVQIRAE IDAVASGAWD RIDNPLRNAP HTAAMVCADR
WEHGYSREAA AFPVAGLRHD KYWPPVSRID NVFGDRNLVC SCPSTKDWAE
//
