ID   GCSP_BURP0              Reviewed;         970 AA.
AC   A3P0U7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00711};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine cleavage system P-protein {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711};
GN   OrderedLocusNames=BURPS1106A_4000;
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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:0000255|HAMAP-Rule:MF_00711}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC         glycine + H(+) = (R)-N(6)-(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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00711};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00711};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP-
CC       Rule:MF_00711}.
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DR   EMBL; CP000572; ABN89009.1; -; Genomic_DNA.
DR   RefSeq; WP_004535539.1; NC_009076.1.
DR   AlphaFoldDB; A3P0U7; -.
DR   SMR; A3P0U7; -.
DR   EnsemblBacteria; ABN89009; ABN89009; BURPS1106A_4000.
DR   GeneID; 56527790; -.
DR   KEGG; bpl:BURPS1106A_4000; -.
DR   HOGENOM; CLU_004620_1_1_4; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000006738; Chromosome I.
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; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
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   PANTHER; PTHR11773; PTHR11773; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR00461; gcvP; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..970
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045574"
FT   MOD_RES         723
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   970 AA;  104036 MW;  737CC68C04B9E47E CRC64;
     MKLEHPDRLM NRTPLSLAAL ETHDAFAERH IGPDAASQQA MLDTLGFATR AALIDAVIPA
     SIRRAETLPL GPFAQPKSEA EALAALRALA DKNQVFRSYI GQGYYDTHTP AVILRNVLEN
     PAWYTAYTPY QPEISQGRLE ALLNFQQMVA DLTGLEISNA SLLDEATAAA EAMTLLQRVG
     KPQSNVFYVA DDVLPQTLEV IKTRAKPIGI EVKSGPAADA AAANAFGVLL QYPGANGDVR
     DYRALADAIH AAGGHVVVAA DILALTVLMP PGEWGADVAV GNTQRFGVPM GFGGPHAAYM
     AVRDEFKRQM PGRLVGVTVD AQGKPALRLA LQTREQHIRR EKATSNVCTA QALLAIMASM
     YAVYHGPRGL KTIALRVNRI AALLAAGIRH LGYATVNDTF FDTLTIDTGA RTAQLHAFAQ
     AKRINLRRAG DTRVGVSVDE TTTRADLADL LTIFAQAAGA TAPDIDALDA GLLPAPALPP
     SLERTSAYLT HHVFNRHHSE TEMLRYLRSL SDKDLALDRS MIPLGSCTMK LNATSEMLPV
     TWPEFGRIHP FAPAEQTVGY REMIDQLEQM LVAATGYAAV SLQPNAGSQG EYAGLLIIHA
     YHESRGESHR DVCLIPASAH GTNPASAHMA GMKVVVVACD AQGNVDIADL KAKADAHSHD
     LAAIMITYPS THGVFEQNVR EICEIVHAHG GQVYVDGANM NAMVGLTAPG QFGGDVSHLN
     LHKTFCIPHG GGGPGVGPHL AKFLPNQRST GYARGEDGIG AVSAAPYGSA SILPISWMYI
     AMMGAKNLTA ATETAILNAN YIAKRLAPHY PVLYSGPGGL VAHECILDLR PIKDSSGITV
     DDVAKRLMDY GFHAPTMSFP VPGTLMVEPT ESESQEELDR FIAAMIAIRD EIRAVEEGRA
     DREDNPLRHA PHTAAVVTAN EWPHAYSREQ AAFPVASLVA NKYWPPVGRA DNAYGDRNLF
     CSCVPVSDYA