ID A0A0Q7A8T7_9BURK Unreviewed; 969 AA.
AC A0A0Q7A8T7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=ASC76_16570 {ECO:0000313|EMBL:KQW36307.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW36307.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW36307.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW36307.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW36307.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW36307.1,
RC ECO:0000313|Proteomes:UP000051611};
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:KQW36307.1}.
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DR EMBL; LMDS01000005; KQW36307.1; -; Genomic_DNA.
DR RefSeq; WP_056468711.1; NZ_LMDS01000005.1.
DR AlphaFoldDB; A0A0Q7A8T7; -.
DR STRING; 1736528.ASC76_16570; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000051611; 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; 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|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000051611}.
FT DOMAIN 21..443
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 483..747
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 780..910
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 969 AA; 103473 MW; CDBD974A7772675F CRC64;
MLMSATKPLR ELENASEFVA RHIGIEADDE RHMLSVIGAA SRRALIEAIV PRGIVRGAPM
ALPEPLTEAQ ALAELKAIAG QNRLLKSFIG QGYHGTHTPG VILRNILENP AWYTAYTPYQ
AEISQGRMEA LVNFQTLVCD LTGMAIAGSS MLDEATAAAE AMTLAMRVGK SKSTTLFVAD
DVLPQTLEVI RTRATPIGVE VVVGAAEDAA HAQAFAVLLQ YPGVDGVVRE LKPIIDAVHA
RGGLAIVAAD LLALTLLAAP GEIGADIVVG NTQRFGMPMG NGGPHAAYLA TRDEFKRSMP
GRLVGVSIDA HGAPAYRLAL QTREQHIRRE KATSNICTAQ VLPAVVASMY AVYHGPDGLK
RIARRVASYT AILAAGLKDM GRTLLSESAF DTLAVNTGDH TDALLQAARD AGFNLRRSSA
CSIGITLNET TTRDDITALW SLFAVGHRLP EFEPFEKGVA SLIPPALQRA SAFMTHPVFN
RHHSETEMLR YIRSLSDKDL ALDRSMIPLG SCTMKLNATS EMIPITWPEF ANIHPFAPQD
QLAGYEQLRV QLEDWLCQAT GYSGVSLQPN AGSQGEYAGL LVIRAFHAAR NEAHRTICLI
PESAHGTNPA SAQMAGLQVV VTKCDADGNI DLADLRAKCE QHSAKLACIM ITYPSTYGVF
DTHVKEICAL VHRHGGRVYV DGANMNALVG VAAPGEFGGD VSHLNLHKTF CIPHGGGGPG
VGPTCVVADL VPYLPAHRAA GIGTDAQVGA VSAAPLGNAA VLPISWMYMR MMGSEGLTAA
TETAILSANY IAARLADHYD IHFSGNIDGI KGGGVAHECI LDLRPLKDAT GGANGVSAED
VAKRLIDYGF HAPTLSFPVA GTLMVEPTES ESLEELDRFC DAMIAIRGEI AKVESGAWPR
DDNPLKAAPH TAGALLKADW PHAYSREEAA YPLASLRRSK YWSPVGRVDN VYGDRNLFCA
CPPLSAYED
//
