GCSP_LEPIC
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 25-MAY-2022, 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}; OrderedLocusNames=LIC_10309;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; 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=(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; AE016823; AAS68936.1; -; Genomic_DNA.
DR RefSeq; WP_001089345.1; NC_005823.1.
DR AlphaFoldDB; Q72VI8; -.
DR SMR; Q72VI8; -.
DR PaxDb; Q72VI8; -.
DR EnsemblBacteria; AAS68936; AAS68936; LIC_10309.
DR GeneID; 61143664; -.
DR KEGG; lic:LIC_10309; -.
DR HOGENOM; CLU_004620_3_2_12; -.
DR OMA; CVPMSEY; -.
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; 3.40.640.10; -; 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..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
