ID GCSP_BURM7 Reviewed; 975 AA. AC A3MQP3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 27-MAR-2024, entry version 92. 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=BMA10247_3058; OS Burkholderia mallei (strain NCTC 10247). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320389; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10247; 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=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; 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}. 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; CP000548; ABO07313.1; -; Genomic_DNA. DR RefSeq; WP_004195877.1; NZ_CP007802.1. DR AlphaFoldDB; A3MQP3; -. DR SMR; A3MQP3; -. DR GeneID; 56594511; -. DR KEGG; bmaz:BM44_298; -. DR KEGG; bmn:BMA10247_3058; -. DR PATRIC; fig|320389.8.peg.324; -. 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; Pyridoxal phosphate. FT CHAIN 1..975 FT /note="Glycine dehydrogenase (decarboxylating)" FT /id="PRO_1000045571" FT MOD_RES 723 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711" SQ SEQUENCE 975 AA; 104460 MW; F610AD40C9512103 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 GGGPGVGPVA VGPHLAKFLP NQRSTGYARG EDGIGAVSAA PYGSASILPI SWMYIAMMGA KNLTAATETA ILNANYIAKR LAPHYPVLYS GPGGLVAHEC ILDLRPIKDS SGITVDDVAK RLMDYGFHAP TMSFPVPGTL MVEPTESESQ EELDRFIAAM IAIRDEIRAV EEGRADREDN PLRHAPHTAA VVTANEWPHA YSREQAAFPV ASLVANKYWP PVGRADNAYG DRNLFCSCVP VSDYA //