ID   GCSP_HAHCH              Reviewed;         960 AA.
AC   Q2SFI6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=HCH_03861;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(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; CP000155; ABC30588.1; -; Genomic_DNA.
DR   RefSeq; WP_011397655.1; NC_007645.1.
DR   AlphaFoldDB; Q2SFI6; -.
DR   SMR; Q2SFI6; -.
DR   STRING; 349521.HCH_03861; -.
DR   KEGG; hch:HCH_03861; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000000238; 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:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 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; Reference proteome.
FT   CHAIN           1..960
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000083208"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   960 AA;  104373 MW;  E6D614BD4A1102B8 CRC64;
     MSDTRETLAE LEQRDAFIGR HIGPDEAEKT AMLNALGVAD METLISKTVP ETIRIKEGLE
     LDGPCTEAQA LAELKAFAER NKVFKTYIGM GYYNTLTPTV ILRNVLENPA WYTAYTPYQP
     EISQGRLEAL LNFQTMIGDL TGMEMANASL LDEGTAAAEA MTMCRRVNGK NKSNVFFVAE
     DCLPQTIEVV KGRAEPLGIE VVVGDPQKDL QNHDYFAVLL QYPGVNGDVR DYRELIKTAH
     ESNALAIMAA DILSLTLLTP PGELGADIAI GNSQRFGVPL FFGGPHAAYI ATKDEYKRSL
     PGRLVGVSVD ANGDKAYRLA LQTREQHIRR QNATSNICTA QALLAITASM YGAYHGPEGL
     KRIARRVHRL TTILAEGLKQ AGRSVNTAHF FDTVSVATGG DTDAVYQAAL QQKINLRRID
     DNTLGVSLDE TTTREDVAAL LHVFASGKPV ADVATLDSSA KDAIPAELRR QSAFMTHTVF
     NRYHSETEML RYLRRLSDKD LALDRTMIPL GSCTMKLNAT TEMTPVSWDG FCAIHPFAPL
     DQTEGYRALI ADLERMLSAA TGYAAFSLQP NAGSQGEYAG LLAIRAYHHS RGEGDRDVCL
     IPNSAHGTNP ASAQMVGMKV VAVKCDDNGN VDLNDLRLKA EQHSAKLAAL MATYPSTHGV
     FEEGIREVCS IVHQHGGQVY IDGANLNAMV GLCKPGQFGG DVSHLNLHKT FCIPHGGGGP
     GVGPIGVAAH LAPFLPGHSA MGETADKAIA PISAAPWGSA GILPISWTYI RMMGGEGLTE
     ATKSAILNAN YIAKRLEPHY PVLYTGSQGF VAHECIIDVR PFKDSCGVTV DDIAKRLIDF
     GFHAPTMSFP VPGTLMIEPT ESESLAELDR FCDAMIAIRE EIRAIENGEY DVDHSPLHHA
     PHTAADLVGD WDRPYSRERG VYPLKALKAD KYWSPVGRID NVYGDRNLVC ACPPMTEYED
//