ID A0A147GLG9_9BURK Unreviewed; 965 AA.
AC A0A147GLG9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=NS331_23875 {ECO:0000313|EMBL:KTT14195.1};
OS Pseudacidovorax intermedius.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pseudacidovorax.
OX NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT14195.1, ECO:0000313|Proteomes:UP000072741};
RN [1] {ECO:0000313|EMBL:KTT14195.1, ECO:0000313|Proteomes:UP000072741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS331 {ECO:0000313|EMBL:KTT14195.1,
RC ECO:0000313|Proteomes:UP000072741};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:ARBA00033655, 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:KTT14195.1}.
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DR EMBL; LDSL01000191; KTT14195.1; -; Genomic_DNA.
DR RefSeq; WP_058644413.1; NZ_LDSL01000191.1.
DR AlphaFoldDB; A0A147GLG9; -.
DR PATRIC; fig|433924.3.peg.2014; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000072741; 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:UP000072741}.
FT DOMAIN 20..446
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 616..744
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 782..903
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 712
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 965 AA; 103679 MW; E4B1D7B758F55838 CRC64;
MSSSAFSLRD LENPTEFIAR HIGPDAEAEA RMLATVGESS RAQLIDSIVP PSIRRSQPMQ
LPPAVSEAEA LAELKAIAAK NQRVKSFIGQ GYHGTHTPGV ILRNVLENPA WYTAYTPYQA
EISQGRMEAL VNFQTMVTDL TGMAIANASM LDEATAAAEA MTLAKRSVKS RSQRFVVAGD
AHPQTIEVIQ TRAAPLGIEV VLANSLQEWN DLLAGDYFAV LAQYPATSGR IDDLRADAEL
IHGKQAALIV ATDLLALTLI APPGEWGADI VVGNTQRFGM PMGAGGPHAA FMACRDEFKR
SLPGRLVGVS VDSHGAPAYR LALQTREQHI RREKATSNIC TAQVLPAVVA SMYAVYHGPA
GLTRIARRVA AYTAILAAGL KQLGAPLREV PSFDTLSLHT KDRTQAILAK ALSLGANLRV
YFGEYLCIAL DETTTRADLA LVWQAFAADG QALPRVEDFE ADVPSLIPAG LQRTSAFLTH
PVFNTHHSET AMLRYIRSLS DKDLALDRSM IPLGSCTMKL NATSEMIPIT WPEFADVHPF
APPSQLAGYA ELDAQLRDWL CQATGYAGIS LQPNAGSQGE YAGLLAIKAW HESRGESHRN
VCLIPSSAHG TNPASAQMVG MQVVVTACDA SGNVDIDDLK RACEKHGDRL ACIMITYPST
HGVFETRVKE LCEIVHAHGG RVYVDGANMN ALVGVAAPGE FGGDVSHLNL HKTFCIPHGG
GGPGVGPVCV VEDLVPFLPG HATGGRPATV GAVSAAPFGN AAVLPISWMY IRMMGAEGLK
QATETAILNA NYISARLADH YPTLYASANG HVAHECILDL RGLKESSGVM AEDVAKRLID
YGFHAPTLSF PVANTLMVEP TESEPLAEMD RFIDAMIAIR GEIRRIEEGV WPREDNPLKN
APHTAATLAA TDWAHPYSRE VAAFPVATLR QAKYWPPVGR VDNVYGDRNL FCSCVPVSEL
QDESA
//