ID M6DF77_9LEPT Unreviewed; 962 AA.
AC M6DF77;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:EMJ99913.1};
GN ORFNames=LEP1GSC192_0904 {ECO:0000313|EMBL:EMJ99913.1};
OS Leptospira sp. B5-022.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1242992 {ECO:0000313|EMBL:EMJ99913.1, ECO:0000313|Proteomes:UP000011981};
RN [1] {ECO:0000313|EMBL:EMJ99913.1, ECO:0000313|Proteomes:UP000011981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B5-022 {ECO:0000313|EMBL:EMJ99913.1,
RC ECO:0000313|Proteomes:UP000011981};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Galloway R.L., 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:EMJ99913.1}.
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DR EMBL; ANIJ01000018; EMJ99913.1; -; Genomic_DNA.
DR RefSeq; WP_020769690.1; NZ_ANIJ01000018.1.
DR AlphaFoldDB; M6DF77; -.
DR STRING; 1242992.LEP1GSC192_0904; -.
DR PATRIC; fig|1242992.3.peg.1914; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000011981; 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; IPR000192; Aminotrans_V_dom.
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; PF00266; Aminotran_5; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR Pfam; PF02347; GDC-P; 1.
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 27..452
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 595..718
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 783..904
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 711
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 962 AA; 105445 MW; FF063977EDEC2D3D CRC64;
MSTATWNGSG KQTEMKNPLD PLDTFPRRHI GPDEDQTKEM LSTLGLSALD ELVAKAVPEG
IRLEKALDLP KASTERKILN DLKKIASKNK LYRSYIGSGY QASVMPGVIQ RNILENPGWY
TAYTPYQAEI SQGRLEALLN FQTMIMDLTG LEIANASLLD EATAAAEAVF LAFGIRKNET
SKLLFISELC HPQTIDVVRT RALPLGIEVK VGSHLNAELN EDYFAVLVQY PGTEGTIYNY
ESFFQLAHTV GALTICAADL LSLTVLKAPG EFGTDIAVGS SQRFGLPYGF GGPHAGYFAT
KDEFKRNMPG RLVGVSKDSQ GNPGLRLSLQ TREQHIRRDK ATSNICTAQV LLAVLSSMYA
VYHGPKGLKD IALRVHRLTE TLAKNLEKAG LAILNKTFFD TIVLDLGSKA ETYLDAASKK
EINFRNLGNG RIAIALDETV EFSDLEDILS VFGISKIDLS LEGISIPNEF VRTSKYLTHP
VFNSHHTETK MLRYIRKLES RDLSLTTSMI PLGSCTMKLN ATVEMFPVTW PEFSNIHPFA
PASQTEGYRT VFSQLESWLS QVTGFPGISL QPNAGSQGEY AGLLAIRNYH ISRGDKNRDI
CLIPISAHGT NPASAAMVGF KVVVVACDSE GNVDLEDLKA KAKEHSKNLA ALMITYPSTH
GVYEEPIKEI CSIIHENGGQ VYMDGANMNA QVGITRPANI GADVCHLNLH KTFCIPHGGG
GPGVGPIGVA EHLKPFLPGH PLVDNGTGNE HGAVSAAPWG SASIVLISWV YIALLGTEGL
EQATKAAILN ANYIAKRLEN YFPVLYKGKN GFVAHECILD VRPFKKTSGV EVEDIAKRLM
DYGFHAPTMS FPVPGTLMIE PTESESQEEL DRFCEAMISI HAEIQEIEQG KADLKDNPLK
NAPHTSAMVI SDNWNHAYSR EQAAYPAPWT KEHKFWPYVG RIDNVYGDRN LVCSCLPPEA
YL
//
