ID   GCSP_LEPBJ              Reviewed;         964 AA.
AC   Q04PM7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
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=LBJ_2732;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000350; ABJ77143.1; -; Genomic_DNA.
DR   RefSeq; WP_011669375.1; NC_008510.1.
DR   AlphaFoldDB; Q04PM7; -.
DR   SMR; Q04PM7; -.
DR   KEGG; lbj:LBJ_2732; -.
DR   HOGENOM; CLU_004620_3_2_12; -.
DR   Proteomes; UP000000656; Chromosome 1.
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_1000045587"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
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;  106287 MW;  04E09A3DD637E767 CRC64;
     MNSTLQNRNR TNLERVSTDP LDTFPRRHIG PDSQQVDKML KSLGLSSLEE LVDKAVPAGI
     RLKKEPDLPK ASTEHKILQD LKNIASQNQI FRSYIGAGYN ACIIPGVIQR NILENPGWYT
     AYTPYQAEIS QGRLEALLNF QTMIIDLTGL EISNASLLDE GTAAAEAMFL AYSIRKNEIA
     KKFFVSELCH PQTIDVVVTR ANPLGIEIVI GNHESVELNE DFFGVLLQYP ATDGKIIDYT
     SFIQRAHNVG AISTVAADLL ALTLLKSPGE MGADIAVGSS QRFGLPLGFG GPHAGYFATK
     DEFKRSMPGR LIGVSKDSQG NPGLRLSLQT REQHIRRDKA TSNICTAQVL LAVISSMYAV
     YHGPEGLKDI ATRIHKFTSI LADALKSSGF TISNDTFFDT ITIQAGAKAK DILNRARSER
     INLREYKDGR IGIALDETVN SDDIKDLFKI FEVKNTDIEK LFSNSGNISD SFKRSTSYLT
     HPVFQSFHTE TKMLRYIRKL ESRDLSLTTS MIPLGSCTMK LNATTEMYPV TWPEFGAIHP
     FAPSEQTKGY KIIFEQLEKW LCEITGFAGV SLQPNAGSQG EYAGLLAIRR YHESRKETHR
     NVCLIPISAH GTNPASAAMA GFKVVVVSCD QNGNVDLEDL KIKAEEHKND LAALMITYPS
     THGVFEESVK EICQIVHSRG GQVYMDGANM NAQVGLTSPG EIGADVCHLN LHKTFCIPHG
     GGGPGVGPIG VAKHLVPFLP GHVLVDNTTG NEHGAVSAAP WGSASIVLIS WIYIALMGSE
     GLTNATRISI LNANYIAKRL EKAYPVLYKG KNGFVAHECI LDVRPFKKSA EIEVEDVAKR
     LIDYGFHAPT MSFPVPGTLM IEPTESESLE ELDRFCEAML LIHQEILDVQ NGTLDKIDNP
     LKNSPHTAAM TTSDRWDHLY PKERAAYPAP WSRDHKFWPF VGRVDNVYGD RNLVCSCLPV
     ESYQ
//