ID A0A9X1YKD9_9BURK Unreviewed; 976 AA.
AC A0A9X1YKD9;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
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 ECO:0000313|EMBL:MCK9685987.1};
GN ORFNames=LPC04_09730 {ECO:0000313|EMBL:MCK9685987.1};
OS Scleromatobacter humisilvae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Sphaerotilaceae; Scleromatobacter.
OX NCBI_TaxID=2897159 {ECO:0000313|EMBL:MCK9685987.1, ECO:0000313|Proteomes:UP001139353};
RN [1] {ECO:0000313|EMBL:MCK9685987.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BS-T2-15 {ECO:0000313|EMBL:MCK9685987.1};
RA Mieszkin S., Alain K.;
RT "BS-T2-15 a new species belonging to the Comamonadaceae family isolated
RT from the soil of a French oak forest.";
RL Submitted (NOV-2021) 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=N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein]
CC + glycine + H(+) = N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; 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:ARBA00049026, 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:MCK9685987.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAJLJH010000002; MCK9685987.1; -; Genomic_DNA.
DR RefSeq; WP_275682021.1; NZ_JAJLJH010000002.1.
DR AlphaFoldDB; A0A9X1YKD9; -.
DR Proteomes; UP001139353; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:TreeGrafter.
DR GO; GO:0016594; F:glycine binding; IEA:TreeGrafter.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR FunFam; 3.40.640.10:FF:000005; Glycine dehydrogenase (decarboxylating), mitochondrial; 1.
DR FunFam; 3.40.640.10:FF:000007; glycine dehydrogenase (Decarboxylating), mitochondrial; 1.
DR FunFam; 3.90.1150.10:FF:000007; Glycine dehydrogenase (decarboxylating), mitochondrial; 1.
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|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00711}; Reference proteome {ECO:0000313|Proteomes:UP001139353}.
FT DOMAIN 21..443
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 613..736
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 782..908
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 708
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 976 AA; 103948 MW; 38773D16B1D50059 CRC64;
MSLTAPTPLA ELENAAEFIA RHIGPDSSDE TQMLSVIGAA SREALISALV PANIVRDAAM
AIPDGTTEAK ALAELKALAG KNQVLKSFIG QGYFGTITPG VILRNILENP AWYTAYTPYQ
AEISQGRMEA LLNFQTMVTD LTGMAIANAS MLDEATAAAE AMTLAMRMGK SKSKVFFVAD
DVLPQTLEVV QTRARPIGIE VVVGPAEQAA DKDCFAALFQ YPGVTGQVRV LKPLVDAIHA
RNGLVIVAAD LLALTLLQAP AEFGADIACG NTQRFGMPMG AGGPHAAYLA TQDALKRSLP
GRLVGVSVDS HGAPAYRLAL QTREQHIRRE KATSNICTAQ VLPAVIASMY AVYHGPEGLR
RIARRVASFT AIFAAGLKLR GVDVVNAHAF DTLEIVTGPQ TDAVLARAVS AHMNLRRASA
TTVSVSFDET TTRACVATLW GIFAPGQTPP TFDAFEQGIE LRLPAELVRT SGFLAHPVFN
THHSETEMLR YIRRLSDKDL ALDRSMIPLG SCTMKLNATS EMIPITWPEF AHVHPFAPAD
QLEGYKLLDE QLCKWLEQAT GYAGISLQPN AGSQGEYAGL LVIKAWHESR GEGSRDVCLI
PESAHGTNPA SAQMVGMKVV VVKCTPAGEV DMADLEAKCI AHKDDLAAMM ITYPSTYGVF
EPGVKALCAL VHQYGGRVYV DGANMNAMVG VAAPGQFGGD VSHLNLHKTF CIPHGGGGPG
VGPVCVVEDL VPFLPAHRSG GLGADDTRRV GAVSAAPLGN AAVLPISWMY VRMMGAAGLK
QATETAILNA NYIAARLSGH YDIHFSGGVA GIKGGGVAHE CILDLRPLKD SSGISAEDVA
KRLIDYGFHA PTLSFPVAGT LMVEPTESEP LVELDRFCDA MIAIRAEIAK VEQGSWPRED
NPLKNAPHTA QALLKAEWPH AYTREDAAYP VTALRLGKYW SPVGRVDNVY GDRNLFCSCV
PMSDFAEAAE AEAAQA
//
