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   27-MAR-2024, entry version 106.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase 2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) 2 {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP2 {ECO:0000255|HAMAP-Rule:MF_00711};
GN   OrderedLocusNames=CPS_3846;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
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 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 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}.
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DR   EMBL; CP000083; AAZ27773.1; -; Genomic_DNA.
DR   RefSeq; WP_011044594.1; NC_003910.7.
DR   AlphaFoldDB; Q47XG2; -.
DR   SMR; Q47XG2; -.
DR   STRING; 167879.CPS_3846; -.
DR   KEGG; cps:CPS_3846; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   Proteomes; UP000000547; Chromosome.
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:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 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..956
FT                   /note="Glycine dehydrogenase (decarboxylating) 2"
FT                   /id="PRO_0000227101"
FT   MOD_RES         706
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
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
//