ID   GCSP_JANSC              Reviewed;         943 AA.
AC   Q28L73;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 91.
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}; OrderedLocusNames=Jann_3622;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia; unclassified Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA   Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000264; ABD56539.1; -; Genomic_DNA.
DR   RefSeq; WP_011456739.1; NC_007802.1.
DR   AlphaFoldDB; Q28L73; -.
DR   SMR; Q28L73; -.
DR   STRING; 290400.Jann_3622; -.
DR   EnsemblBacteria; ABD56539; ABD56539; Jann_3622.
DR   KEGG; jan:Jann_3622; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000008326; 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; 3.40.640.10; -; 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; Reference proteome.
FT   CHAIN           1..943
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045585"
FT   MOD_RES         695
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   943 AA;  101257 MW;  962EB20AE215A569 CRC64;
     MPWTTTDYDP TDFANRRHIG PSPAEMAEML EFVGADSLDA LIDDTVPASI RQAGALDWAA
     MSEAELLDHM RAIADKNKPM VSMIGQGYFG THTPPAIQRN VLENPAWYTA YTPYQPEIAQ
     GRLEALLNFQ TMVADLTGLP VANASLLDEA TAAAEAMVMA QRASKSKART FFVDETCHPQ
     TIAVIQTRAE PLGIEVRVGD AAMLDADAVF GAIFQYPCTF GGLRDPSAQI EALHEAKAIA
     VVATDLLALT VLKEPGAMGA DIAVGSAQRF GVPLGYGGPH AAFMSCRDAL KRSLPGRIVG
     VSVDSHGQNA YRLSLQTREQ HIRREKATSN VCTAQALLAV MASFYAVFHG PKGLRAIAER
     VHMRAVRLAA SLSAGGFAPD NDTFFDTLTV HVGDKQSRIM AAAVARGINL RDVGADRIGI
     SVDEVTTDAH IEAVCRAFGV LKAPAPKAPA ISDDLLRMSD YLTHPIFHMN RAESEMMRYM
     RRLSDRDLAL DRAMIPLGSC TMKLNAAVEM MPITWPEFGN LHPFAPADQA EGYAEMLEDL
     SAKLCDITGY DAMSMQPNSG AQGEYAGLLT IAAYHRARGE TRNICLIPVS AHGTNPASAQ
     MAGMQVVVVK SQEDGDIDLV DFRAKAEAAG DKLAACMITY PSTHGVFEES VREVCEITHE
     LGGQVYLDGA NLNAMVGLSK PGELGADVSH LNLHKTFCIP HGGGGPGMGP IGVKAHLAPH
     LPGHPETGGT QGPVSAAPYG SASILPISYA YVHLMGGSGL TQATKVAILG ANYIAKRLEG
     DYGVLFKGKT GRVAHECILD TRPFAEAGIT VDDIAKRLMD HGFHAPTMSW PVAGTLMVEP
     TESETKAELD RFITAMQAIR AEIAEVEDGL PAGDSPLHHA PHTMEDLVRD WDRAYTREQG
     CFPPGAFRVD KYWPPVNRVD NVAGDRNLIC TCPPLEEYLD AAE