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Database: UniProt
Entry: A0A147GLG9_9BURK
LinkDB: A0A147GLG9_9BURK
Original site: A0A147GLG9_9BURK 
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
//
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