GCSP_LEPIN
ID GCSP_LEPIN Reviewed; 964 AA.
AC Q8F937;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=LA_0360;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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; AE010300; AAN47559.1; -; Genomic_DNA.
DR RefSeq; NP_710541.1; NC_004342.2.
DR RefSeq; WP_001089349.1; NC_004342.2.
DR AlphaFoldDB; Q8F937; -.
DR SMR; Q8F937; -.
DR STRING; 189518.LA_0360; -.
DR EnsemblBacteria; AAN47559; AAN47559; LA_0360.
DR KEGG; lil:LA_0360; -.
DR PATRIC; fig|189518.3.peg.365; -.
DR HOGENOM; CLU_004620_3_2_12; -.
DR InParanoid; Q8F937; -.
DR OMA; CVPMSEY; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
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..964
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_0000166917"
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; 106320 MW; 629D62D9B17535D7 CRC64;
MNSTLQNQTK TNLEKVGTDP LDTFPRRHIG PNLQQTAEML KELGLSSVEE LIDKAVPVGI
RLKKSLDLPK ASTEHKILQN LKGIASQNQV FRSYIGAGYH SCIIPGVIQR NILENPGWYT
AYTPYQAEIS QGRLEALLNF QTMIIDLTGL EISNASLLDE GTAAAEAMFL AYSVRKNETA
KKFFVSELCH PQTIDVVVTR ANPLGIEVQI GNHESIELNE DFFGVLLQYP ATDGKVIDYT
SFIQRSHNVG AISTVAADLL ALTLLKSPGE MGADIAVGSS QRFGLPLGFG GPHAGYFATK
DEFKRSMPGR LIGVSKDSQG NSGLRLSLQT REQHIRRDKA TSNICTAQVL LAVISSMYAI
YHGPEGLKNI ATRIYKFTSI FANVLKNAGF SITNEFFFDT ITIQAGAKVQ 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 GHVLVNNATG NEHGAVSAAP WGSASIVLIS WVYIALMGSE
GLTNATRNSI LNANYIAKRL EKVYPVLYKG KNGFVAHECI LDLRPFKKSA GIEVEDVAKR
LIDYGFHAPT MSFPVPGTLM IEPTESESLE ELDRFCEAML LIYQEILDVQ NGTLDKTDNP
LKNSPHTAAM VTSDRWDHLY PRERAAYPAS WLKDHKFWPY VGRVDNVYGD RNLVCSCLPI
ESYQ
