ID A0A1E3SPP5_9MYCO Unreviewed; 945 AA.
AC A0A1E3SPP5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ORFNames=AWC25_12765 {ECO:0000313|EMBL:ORW75961.1}, BHQ21_18700
GN {ECO:0000313|EMBL:ODR04126.1};
OS Mycobacterium sherrisii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=243061 {ECO:0000313|EMBL:ODR04126.1, ECO:0000313|Proteomes:UP000094224};
RN [1] {ECO:0000313|EMBL:ORW75961.1, ECO:0000313|Proteomes:UP000193024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-832 {ECO:0000313|EMBL:ORW75961.1,
RC ECO:0000313|Proteomes:UP000193024};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000094224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC1_M4 {ECO:0000313|Proteomes:UP000094224};
RA Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ODR04126.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC1_M4 {ECO:0000313|EMBL:ODR04126.1};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) 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:ODR04126.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MIHC01000035; ODR04126.1; -; Genomic_DNA.
DR EMBL; LQPT01000092; ORW75961.1; -; Genomic_DNA.
DR RefSeq; WP_069401782.1; NZ_MIHC01000035.1.
DR STRING; 243061.AWC25_12765; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000094224; Unassembled WGS sequence.
DR Proteomes; UP000193024; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000094224}.
FT DOMAIN 10..442
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 449..724
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 766..887
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 696
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 945 AA; 99906 MW; D0CA0DF2DEE7270C CRC64;
MPTQAPFSAR HIGPDAAAVS AMLDVIGVGS LDELAGKAVP HRILDKLAAD GTAPGLDSLP
PAATEAEALA ELRALADNNT VAVSMIGQGY YDTLTPPVLL RNILENPAWY TAYTPYQPEI
SQGRLEALLN FQTMITDLTG LEIANASMLD EGTAAAEAMT LLHRSATRRA GTGTNRLAVD
VDLFGQTAAV LATRARPLGI EIVTADLRNG LPDGDFFGVI AQLPGASGRV TDWSALVAEA
HERGALVAIG ADLLACTLIT PPGEIGADAA FGSSQRFGVP MGFGGPHAGY LAVHAKHARQ
LPGRLVGVSV DTDGSPAYRL ALQTREQHIR RDKATSNICT AQVLLAVMAA MYASYHGADG
LTAIARRVHR HATSIAAALG DALVHEEYFD TVLAHVPGCA DEVVAKAKAK GINLWRVDKD
HVSVACDECT TDSHVEEVLD AFGVSAAEPV PTGIGTRTTA FLTHPAFTQY RTETAMMRYL
RTLADKDIAL DRSMIPLGSC TMKLNAAAEM EPITWPEFSR LHPFAPADDT AGLRRLISDL
QSWLVAITGY DAVSLQPNAG SQGEYAGLLA IHEYHASRGE AHRDICLIPS SAHGTNAASA
ALAGMRVVVV GCHDNGDVDL DDLRAKVAEH ADRLAALMVT YPSTHGVYEQ DIAEICAAVH
DAGGQVYVDG ANLNALVGLA RPGKFGGDVS HLNLHKTFCI PHGGGGPGVG PVAARAHLAP
FLPGHPYAPE LPGGHPVSSA PYGSASILPI SWAYIRMMGG DGLRAASLTA IASANYIARR
LDEYFPVLYT GATGMVAHEC ILDLRGITKS TGVTVDDVAK RLADYGFHAP TMSFPVAGTL
MVEPTESEDR NEIDAFCDAM IAIRAEIDKV AAGVWPVEDN PLRGAPHTAD CLLVAQWNHP
YTREEAAYPL GKAFRPKVWP PVRRIDGAHG DRNLMCSCPP VEAFA
//
