ID   GCSP_PSYA2              Reviewed;         965 AA.
AC   Q4FTK9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 112.
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=Psyc_0796;
OS   Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX   PubMed=20154119; DOI=10.1128/aem.02101-09;
RA   Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA   Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA   Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA   Murray A., Thomashow M., Tiedje J.M.;
RT   "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT   Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT   temperature growth.";
RL   Appl. Environ. Microbiol. 76:2304-2312(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}.
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DR   EMBL; CP000082; AAZ18649.1; -; Genomic_DNA.
DR   RefSeq; WP_011280076.1; NC_007204.1.
DR   AlphaFoldDB; Q4FTK9; -.
DR   SMR; Q4FTK9; -.
DR   STRING; 259536.Psyc_0796; -.
DR   KEGG; par:Psyc_0796; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000000546; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
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; PF01212; Beta_elim_lyase; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..965
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227122"
FT   MOD_RES         711
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   965 AA;  105914 MW;  9CC5BCC617624E50 CRC64;
     MTISQNPTLD TFKGLFNEAE FVYRHLGSND AKQADLLSAI GYKDMATFIN DTVPEPVRLH
     KELDLPVAMS EHAALAKLRT MADDITVNKS YIGQGYSPVR MPAVIQRNVL ENPGWYTAYT
     PYQAEIAQGR LEALLNFQQV CIDLTGLELA GASLLDEATA AAEAMAMSKR VSKSKSMQFF
     VDDRVYSQTL DVINTRAKYF GWEVVVGDFE LAKSGDYFGA LFQYVGVEGD VKDLTDVIAA
     VKKNKTYVNV VSDIMSLVLL KSPADMGADV ALGSTQRFGI PMGFGGPHAA YFAFSDKAKR
     SAPGRIIGVS KDSQGNTALR MALQTREQHI RREKANSNIC TSQVLLANLA GMYAVYHGPG
     GVKRIATRIH AFATAFADVI KNANDSNLNV VHDQFFDSVV IDCGSEKLAT QIFENADNVG
     YNLWRLGDSK LSVAFSETSD QEDFKILTQL FVTKAHDLPE DARISLDSTH LRTDDILTHP
     VFNSHHTEHE MLRYLKSLED KDLAMNRSMI SLGSCTMKLN ATSEMLPITW PEFANVHPFA
     PRDQVTGYVA MIDSLQEQLK AITGFDDVSM QPNSGASGEY AGLLAIRRYH ESLGETDRDV
     CLIPMSAHGT NPATAMMMGM KVVVVKTDDN GNVDIDDLTA KSEEHSARLG ALMITYPSTH
     GVFEEGIRKI CDLIHKHGGQ VYMDGANMNA QVGMMQPADV GADVLHMNLH KTFCIPHGGG
     GPGMGPIGMK SHLAPFMANH TLSPVHNAQK DCSAVSAAPY GSASILPISW MYIAMMGRDG
     LLKATELALL NANYVAAELK DYYPVLYTGK NGRVAHECII DIRPLKEETG ISESDIAKRL
     MDYGFHSPTM SFPVAGTLMI EPTESESKEE LDRFISALKS IKAEAMKAKA GEDNWTLENN
     PLVNAPHTAA MVIDGEWTYP YSRETAAFPL PYIRTNKFWP SVARVDDAYG DKNLMCSCPS
     IENYM
//