ID   GCSP_CUTAK              Reviewed;         994 AA.
AC   Q6A9R8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=PPA0742;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT82498.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6A9R8; -.
DR   SMR; Q6A9R8; -.
DR   STRING; 267747.PPA0742; -.
DR   EnsemblBacteria; AAT82498; AAT82498; PPA0742.
DR   KEGG; pac:PPA0742; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_0_11; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000000603; 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; 1.
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.
FT   CHAIN           1..994
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227114"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         716
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   994 AA;  107817 MW;  793F731ED0AAA673 CRC64;
     MTDHAENRCG LEGPRPFSSR HVGSVEDDLR YIAETIGVTS PEQIIRDAIP ASVLDSNEGD
     SSVRTPSFPP AADETTARAE LVEIASGNRV TRALIGRGYY GTLTPPVIRR NILENPSWYT
     AYTPYQPEIS QGRLEMLTIY QQLITDLTGL ALANSSLLDE ATAASEGMLL ARRAARKVKS
     NRFLVHTHLF DQVRDVVLGH AEATGIEVVE TDLRDPQSWR PEVEAGCFGV LAPYPDSTGA
     LWNPSEVFDA VHKVGGITIA ECDLLSLTLL APPGELGADV AVGSSQRFGV PMGNGGPHAA
     YMSVRSGLER QIPGRLVGVS TDADGNPAYR LALQTREQHI RRDKATSNIC TAQVLLAVVA
     AAYAVWHGPT GLTRIARQVT DRAHQLASAL RAAGLDVADQ QFFDTIRIRT KGGAKELWNR
     AREGGYTLDL VDGDILQISV DETVTDDELR ELTQLLGGST DEIRGPADRA WPEDLRRTSS
     FMTHPVFSSY HTETTMMRYL KRLADHDYGL DRGMIPLGSC TMKLNAAAEM EAMTWPAFSQ
     MHPFAPVEDQ AGSLRLIRDL EIWLAELTGY DTVSLQPNAG SQGEYTGLAA IRSYHVSRGD
     TERNVCLVPA SAHGTNAASA ASAGLRVVVV KSNDDGTIDR DDLAAKIAAN EGRIAAIMIT
     YPSTHGVYED GVRQVCDMVH EAGGQVYIDG ANFNALVGWG QFARIGGDVS HLNLHKTFAI
     PHGGGGPGVG PVAAKAHLAP FLPGHPLNPR NEHPLNDGGT VTHDGHAVSA APFGSVSVLP
     ISWAYLRLMG LKGLQFATEV AVLNANYIAH RLHDKIPILY TGQNGYVAHE CILDLRPLTT
     ETGITVDDVA KRLIDYGFHA PTMSFPVAGT LMVEPTESED LAELDRFCDA MLAIVEEARM
     VQSGHWPAND NPLINAPHPA ARLVADEWNH PYSRELGCYP GMRLGIQRDQ ERGLDVNTVT
     RIQAKYWPPV GRVDNTYGDR HLVCSCPPPE AFED