ID   GCSP_LEPIC              Reviewed;         964 AA.
AC   Q72VI8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 110.
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=LIC_10309;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(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=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; AE016823; AAS68936.1; -; Genomic_DNA.
DR   RefSeq; WP_001089345.1; NC_005823.1.
DR   AlphaFoldDB; Q72VI8; -.
DR   SMR; Q72VI8; -.
DR   GeneID; 61143664; -.
DR   KEGG; lic:LIC_10309; -.
DR   HOGENOM; CLU_004620_3_2_12; -.
DR   Proteomes; UP000007037; Chromosome I.
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.
FT   CHAIN           1..964
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166916"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         713
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   964 AA;  106324 MW;  67CEEDC4FE40C401 CRC64;
     MNSTLQNQTK TNLEKVGTDP LDTFPRRHIG PNLQQTAEML KELGLSSVEE LIDKAVPVGI
     RLKKSLDLPK ASTEHKILQN LKGIASQNQV FRSYIGAGYH SCIIPGVIQR NILENPGWYT
     AYTPYQAEIS QGRLEALLNF QTMIIDLTGL EISNASLLDE GTAAAEAMFL AYSVRKNETA
     KKFFVSELCH PQTIDVVVTR ANPLGIEVQI GNHESIELNE DFFGVLLQYP ATDGKIIDYT
     SFIQRSHNVG AISTVAADLL ALTLLKSPGE MGADIAVGSS QRFGLPLGFG GPHAGYFATK
     DEFKRSMPGR LIGVSKDSQG NSGLRLSLQT REQHIRRDKA TSNICTAQVL LAVISSMYAV
     YHGPEGLKNI ATRIYKFTSI FANVLKNAGF SITNEFFFDT ITIQAGTKVQ EILNRAYSKK
     INFREYKDGK IGITLDETVN LEDLKDLLEI FEIKNTDIEK LFVDVSNVPD SFKRKTSYLT
     HPVFQSHHTE TKMLRYIRKL ESRDLSLTTS MIPLGSCTMK LNATTEMYPV TWPEFGAIHP
     FAPADQTKGY KIIFEQLEKW LCEITGFAGV SLQPNAGSQG EYAGLLAIRR YHESRNESYR
     NVCLIPISAH GTNPASAAMA GFQVVVVSCD PNGNVDLEDL KAKAEEHKKD LAALMITYPS
     THGVFEESVK EICQIVHSCG GQVYMDGANM NAQVGLTSPG EIGADVCHLN LHKTFCIPHG
     GGGPGVGPIG VAKHLVPFLP GHVLVDNATG NEHGAVSAAP WGSASIVLIS WVYIALMGSE
     GLTNATRNSI LNANYIAKRL EKVYPVLYKG KNGFVAHECI LDLRPFKKSA GIEVEDVAKR
     LIDYGFHAPT MSFPVPGTLM IEPTESESLE ELDRFCEAML LIYQEILDVQ SGTLDKTDNP
     LKNSPHTAAM VTSDRWDHLY PRERAAYPAS WLKDHKFWPY VGRVDNVYGD RNLVCSCLPI
     ESYQ
//