ID GCSP2_COLP3 Reviewed; 956 AA. AC Q47XG2; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=Glycine dehydrogenase [decarboxylating] 2; DE EC=1.4.4.2; DE AltName: Full=Glycine decarboxylase 2; DE AltName: Full=Glycine cleavage system P-protein 2; GN Name=gcvP2; OrderedLocusNames=CPS_3846; OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio OS psychroerythus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=167879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16043709; DOI=10.1073/pnas.0504766102; RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B., RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.; RT "The psychrophilic lifestyle as revealed by the genome sequence of RT Colwellia psychrerythraea 34H through genomic and proteomic RT analyses."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005). CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. The P protein binds the alpha-amino group of glycine CC through its pyridoxal phosphate cofactor; CO(2) is released and CC the remaining methylamine moiety is then transferred to the CC lipoamide cofactor of the H protein (By similarity). CC -!- CATALYTIC ACTIVITY: Glycine + H-protein-lipoyllysine = H-protein- CC S-aminomethyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H (By similarity). CC -!- SIMILARITY: Belongs to the gcvP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000083; AAZ27773.1; -; Genomic_DNA. DR RefSeq; YP_270508.1; -. DR GeneID; 3522032; -. DR GenomeReviews; CP000083_GR; CPS_3846. DR KEGG; cps:CPS_3846; -. DR NMPDR; fig|167879.3.peg.3336; -. DR TIGR; CPS_3846; -. DR HOGENOM; Q47XG2; -. DR OMA; Q47XG2; ANGEYAG. DR BioCyc; CPSY167879:CPS_3846-MON; -. DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) act...; IEA:EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavag...; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00711; -; 1. DR InterPro; IPR003437; GDC-P. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 2. DR PANTHER; PTHR11773; GDC-P; 1. DR Pfam; PF02347; GDC-P; 1. DR TIGRFAMs; TIGR00461; gcvP; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Pyridoxal phosphate. FT CHAIN 1 956 Glycine dehydrogenase [decarboxylating] FT 2. FT /FTId=PRO_0000227101. FT MOD_RES 706 706 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 956 AA; 105128 MW; B37425159D3F1048 CRC64; MTNNNLLAQL NDNLDFISRH NGPDRTQQQH MLDTLKVDSI EQMIDKTVPD NIRLLQPMAL AKPQSEIEML ATLKGIASKN KVNRSYIGQG YYDTHVPHVI LRNVFENPGW YTAYTPYQPE ISQGRLEALL NFQQMITDLT AMELSNASLL DEATAAAEAM SLCKRASKNK SNVFFVSDDV HPQTLDVINT RAKYFSFEVV VAPCSELENH DVFGALLQYP GTTGQVHNLE KIIEQAHSKK TLVAVAADLL ALTVLKAPGE MGADVVIGSA QRFGVPMGYG GPHAAFMATK EKYKRTIPGR VIGVSIDSKG KPALRMAMQT REQHIRREKA NSNICTAQAL LANMASFYAV YHGPQGLRKM GRRVNRLTSV LAAGLQKAGI ELVHNDFFDT ITLQTNEKTD AIYQRALAAD LNLRLLPDQL GISLDETTTS ADVEALWLAI TEQSFNVDDI EQTLSAEFCN IPADCQRTSE YLSHPVFNSY HSETRMLRYL KSLENKDFSL THGMIPLGSC TMKLNATAQM IPVTWPEFSR MHPFAPSDQC TGYETLAESF SDMLIEITGY DAFSLQPNSG AQGEYAGLIA IQRYHASRGE DYRNICLIPS SAHGTNPASA SMVSMRIVLV NCDKEGNVDL DDLKEKINLH RDQLSAMMIT YPSTHGVYEE SIKEICELIH EAGGQVYLDG ANMNAQVGLT SPGFIGADVS HLNLHKTFCI PHGGGGPGMG PIGVKSHLAD FLPGHSVTNT VGAVSATALG SASILPISWA YIALMGAEGL KSATELAILN ANYIMEKLSP HYPILFRGKQ GRVAHECIID LRPLKESSGI SEEDVAKRLM DFGFHAPTMS FPVAGTLMIE PTESESLEEL DKFIDALITI RHEIAKVEEG TWTLADNPLV NAPHTLNDLT GSDWPRAYSR LTACYPSSCP SQPKFWPTTN RIDNVYGDRN LICSCPPIES YQSTDT //