ID M6YMF8_9LEPT Unreviewed; 964 AA.
AC M6YMF8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711,
GN ECO:0000313|EMBL:EMO87488.1};
GN ORFNames=LEP1GSC024_0988 {ECO:0000313|EMBL:EMO87488.1};
OS Leptospira noguchii str. 2001034031.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193053 {ECO:0000313|EMBL:EMO87488.1, ECO:0000313|Proteomes:UP000012138};
RN [1] {ECO:0000313|EMBL:EMO87488.1, ECO:0000313|Proteomes:UP000012138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2001034031 {ECO:0000313|EMBL:EMO87488.1,
RC ECO:0000313|Proteomes:UP000012138};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Whelen A.C., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMO87488.1}.
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DR EMBL; AKXB02000151; EMO87488.1; -; Genomic_DNA.
DR RefSeq; WP_004447455.1; NZ_AKXB02000151.1.
DR AlphaFoldDB; M6YMF8; -.
DR Proteomes; UP000012138; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50}.
FT DOMAIN 26..451
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 457..744
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 785..906
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
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:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 964 AA; 106411 MW; D0DB40F40F57836E CRC64;
MNSTLQNQTK TNLEKVGTDP LDTFPRRHIG PDLQQTAEML KELGLSSVEE LINKSVPAGI
RLKKSLDLPK ASTEHKILQD LKGIASQNQV FRSYIGAGYY SCIIPGVIQR NILENPGWYT
AYTPYQAEIS QGRLEALLNF QTMIIDLTGL EISNASLLDE GTAAAEAMFL AYSVRKNETA
KKFFVSELCH PQTIDVVVTR ANPLGIEVHI GDHESIELNE DFFGVLLQYP ATNGKVIDYT
SFIQIAHNVG ALSTIAADLL ALTLLKSPGE MGADIAVGSS QRFGLPLGFG GPHAGYFATK
DEFKRSMPGR LIGVSKDSQG NPGLRLSLQT REQHIRRDKA TSNICTAQVL LAVISSMYAI
YHGPEGLKNI ATRIYKFTSI FANVLKNAGF TITNDSFFDT ITIQTGTKTQ EILNRARSQK
INFREYKDGR IGITLDETVN SKDLKDLLEI FELKNTDIEK LFVDAQNIPE SLNRKTSYLT
HPVFQSYHTE TKMLRYIRKL ESRDLSLTTS MIPLGSCTMK LNATTEMYPV TWPEFGAIHP
FAPADQTKGY KIIFEQLEKW LCEITGFAGV SLQPNAGSQG EYAGLLAIRR FHESRNESYR
NVCLIPISAH GTNPASAAMA GFQVVVVSCD QNGNVDLEDL KAKAEEHKKD LAALMITYPS
THGVFEESVK EICQIVHSCG GQVYMDGANM NAQVGLTSPG EIGADVCHLN LHKTFCIPHG
GGGPGVGPIG VAKHLVPFLP GHVLINNKTG NEHGAVSAAP WGSASIILIS WVYIALMGSE
GLTNATRNSI LNANYIAKRL EKVYPVLYKG KNGFVAHECI LDLRPFKKSA GIEVEDVAKR
LIDYGFHAPT MSFPVPGTLM IEPTESESLE ELDRFCEAML LIFQEILDVQ NGILDKTDNP
LKNSPHTAAM VTSDRWDHLY SRERAAYPAS WLKDHKFWPY VGRVDNVYGD RNLVCSCLPI
ESYQ
//
