ID A0A328YHD2_9BURK Unreviewed; 990 AA.
AC A0A328YHD2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=AX018_10746 {ECO:0000313|EMBL:RAR72960.1};
OS Paracidovorax anthurii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paracidovorax.
OX NCBI_TaxID=78229 {ECO:0000313|EMBL:RAR72960.1, ECO:0000313|Proteomes:UP000248856};
RN [1] {ECO:0000313|EMBL:RAR72960.1, ECO:0000313|Proteomes:UP000248856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFPB 3232 {ECO:0000313|EMBL:RAR72960.1,
RC ECO:0000313|Proteomes:UP000248856};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-2018) 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:RAR72960.1}.
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DR EMBL; QLTA01000074; RAR72960.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328YHD2; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000248856; 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:UP000248856}.
FT DOMAIN 21..448
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 462..743
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 809..930
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 750..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 714
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 990 AA; 106444 MW; 9E5B84859F17FDAB CRC64;
MPTPTFPPLG ALENAAEFQP RHIGIDAADE QRMLSAIGEA SRAALVESIV PRSIARTAPM
ELPPATTEAA ALAELKAIAS KNRVLKSFIG QGYHGTHTPG VILRNILENP AWYTAYTPYQ
AEISQGRMEA LVNFQTLVCD LTGMPIANAS MLDEATAAAE AMTLAKRSVK SKSQTLVVSG
DTHPQTIEVI RTRAEPLGIA VVVANSEAEW NAALEGDLFA AVIQYPASSG WLADWRADVQ
KIHGKQAAAI VCADLLALTL LVPPGEWDAD IVVGNTQRLG MPMGAGGPHA AFMACRDEFK
RSLPGRLVGV SVDTHGQPAY RLALQTREQH IRREKATSNI CTAQVLPAVV ASMYAVYHGP
EGLTRIAQRV ASYTAILAKG LAALGHTARH HDSAFDTLCL HTKEQTRALL ARALERGANL
RVAWDDYLCI SLDETTTRAD IKLLWSVFAA EGQTLPRVED FEAGVEPLIP AALRRTSSFL
THPVFNTHHS ETGMLRYIRQ LSDKDLALDR SMIPLGSCTM KLNATSEMIP ITWPEFAQVH
PFAPADQLEG YRLLDEQLRA WLCEATGYAG ISLQPNAGSQ GEYAGLLAIR AWHKAQGQGH
RNICLIPSSA HGTNPASAQM VGMQVVVTAC DASGNVDLQD LRAKCEQHAE KLACVMITYP
STHGVFETQV KELCALVHQH GGRVYVDGAN MNAMVGVAAP GAFGGDVSHL NLHKTFCIPH
GGGGPGVGPV CVVEDLIPYL PGHATASAQG ALEPAPGRPK LAKAPSGGSE PHAVGSVGAV
SSAPLGNAAV LPISWMYIRM MGADGLRAAT ETAILSANYI SACLKEHYPT LYASANGHVA
HECILDLRGF KETSGVMAED VAKRLIDYGF HAPTLSFPVP NTLMVEPTES ETLAELDRFI
DAMIAIREEI RRIEQGEWPQ DDNPLKNAPH TAHQLLSGEW QHPYPRETAA YPVAALRHGK
YWAPVGRVDN VYGDRNLFCS CVPVAELAQD
//
