ID W5J0Q5_PSEUO Unreviewed; 953 AA.
AC W5J0Q5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=PM1_0218015 {ECO:0000313|EMBL:ETM68082.1};
OS Pseudomonas sp. (strain M1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=95619 {ECO:0000313|EMBL:ETM68082.1};
RN [1] {ECO:0000313|EMBL:ETM68082.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ETM68082.1};
RX PubMed=10388678;
RA Iurescia S., Marconi A.M., Tofani D., Gambacorta A., Paterno A.,
RA Devirgiliis C., van der Werf M.J., Zennaro E.;
RT "Identification and sequencing of beta-myrcene catabolism genes from
RT Pseudomonas sp. strain M1.";
RL Appl. Environ. Microbiol. 65:2871-2876(1999).
RN [2] {ECO:0000313|EMBL:ETM68082.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M1 {ECO:0000313|EMBL:ETM68082.1};
RA Soares-Castro P.M., Santos P.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETM68082.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ETM68082.1};
RX PubMed=23405299;
RA Soares-Castro P., Santos P.M.;
RT "Towards the Description of the Genome Catalogue of Pseudomonas sp. Strain
RT M1.";
RL Genome Announc. 1:E00146-E00112(2013).
RN [4] {ECO:0000313|EMBL:ETM68082.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M1 {ECO:0000313|EMBL:ETM68082.1};
RA Soares-Castro P., Santos P.M.;
RT "Decyphering the genome repertoire of Pseudomonas sp. M1 towards myrcene
RT biotransformation.";
RL Submitted (DEC-2013) 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:ETM68082.1}.
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; ANIR02000002; ETM68082.1; -; Genomic_DNA.
DR RefSeq; WP_009616870.1; NZ_CP094343.1.
DR AlphaFoldDB; W5J0Q5; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
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}.
FT DOMAIN 15..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 471..732
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 773..894
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 704
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 953 AA; 102551 MW; B2123181958FCB29 CRC64;
MSKVQLSTRN EFIARHIGPR EADTQAMLEL VGYASLDALT DSVIPNSIKG TSVLDGSAGQ
GEAQALADLR AIAAQNQLLR NHIGQGYYPC HTPAPILRNL LENPAWYTAY TPYQPEISQG
RLEALLNFQT LIGDLTGMQI ANASLLDEAT AAAEAMTFCK RLSKNKAAQA FFASAHCHPQ
TLDVLRTRAE PLGIEVVVGD EAALQDFSAY FGVLLQYPAS TGAVIDYREL IERAHAAGTL
VAVAADLLAL TLLTPPGEFG ADVVLGSAQR FGVPLGFGGP HAAYFATRDA FKRDMPGRLV
GISIDRFGNP ALRLAMQTRE QHIRREKATS NICTAQVLLA NIASMYAVYH GPQGLSDIAR
RVHRLTAILA AGLAQLGHKV EQEYFFDTLS VATARPAAEV HAAAQAAGIN LRVIDDGRVG
VSLDETCEQA AVEALWAVFA AGQTLPDFAA LAASVGDQLP QALLRTSAFL RHEVFNRYHS
ETELMRYLRR LADKDLALDR SMIPLGSCTM KLNAASEMIP ITWAEFGNLH PFAPAEQAAG
YRAMTAELEA MLCAATGYDA VSLQPNAGSQ GEYAGLLAIR AYHASRGEGH RDICLIPSSA
HGTNPATAQM AGLRVVVTAC DARGNVDLAD LKAKAEEHRE RLAAIMITYP STHGVFEEAV
RDICAIVHDN GGQVYIDGAN MNAMVGLCAP GRFGGDVSHL NLHKTFCIPH GGGGPGVGPI
GVKAHLAPFL PGHGEQLERK QGAVSAAPFG SASILPITWM YIRMMGGQGL KRASQAAILG
ANYIARRLEE HYPVLYTGEN GLVAHECILD LRPLKETSGI NVDDVAKRLI DFGFHAPTMS
FPVAGTLMVE PTESESKEEL DRFCDAMIRI REEIRAVERG ELDKDDNPLK NAPHTAAELV
GEWSHPYSRE QAVYPLASLV DGKYWPPVGR VDNVYGDRNL ACSCPSIADY QDA
//
