ID U2RSW4_LEIAQ Unreviewed; 915 AA.
AC U2RSW4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=N136_01737 {ECO:0000313|EMBL:ERK71906.1};
OS Leifsonia aquatica ATCC 14665.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1358026 {ECO:0000313|EMBL:ERK71906.1, ECO:0000313|Proteomes:UP000016605};
RN [1] {ECO:0000313|EMBL:ERK71906.1, ECO:0000313|Proteomes:UP000016605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14665 {ECO:0000313|EMBL:ERK71906.1,
RC ECO:0000313|Proteomes:UP000016605};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-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:ERK71906.1}.
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DR EMBL; AWVQ01000212; ERK71906.1; -; Genomic_DNA.
DR AlphaFoldDB; U2RSW4; -.
DR PATRIC; fig|1358026.3.peg.1489; -.
DR HOGENOM; CLU_004620_3_2_11; -.
DR Proteomes; UP000016605; 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; 1.
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:UP000016605}.
FT DOMAIN 1..375
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 426..684
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 736..857
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 655
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 915 AA; 96538 MW; 346B522DC81FE74F CRC64;
MPAPASERAA LRELRAIASR NTVNRSLIGL GYYGTLTPAV IKRNVLENPG WYTAYTPYQP
EISQGRLEAL INFQTMVADL TGLDTANASM LDEGTAVVEG MLLARRASKA ASSRFVVDAD
IFPQTLALLR NRAEAVGIEL IVRDLAATPA DAPELADAFG LFVQYPGASG RVWDPSGVIA
AAKAGGAVVV AAADLLALTQ LRSPGELGAD VAVGTSQRFG VPMGFGGPHA GYMAVRSGLE
RQLPGRLVGV SQDAVGKPAY RLTLQTREQH IRREKATSNI CTAQVLLAVM AAMYAVYHGP
QGLRAIGRQV HLTTAAVADL LRASGVDVVS NSYFDTLQVA VDDAAGVVER AHAHGLLLHA
TDAGLVSLSV DEEVAADLRD GDFPLADLVE VLGGTVDSAP ELSLPAEASF DGALARTSAY
LTHPVFNTHH SETAMMRYLR QLQDRDYALD RGMIPLGSCT MKLNAATEME AVTWPEFAAL
HPFAPAADVQ GSLALIDQLE AWLADVTGYD TVSLQPNAGS QGELAGLLAI RGYHRSRGDG
QRTVCLIPQS AHGTNAASAV LAGMRVVVVA TDDLGNVDLD DLRAKIAEHA ETLAALMITY
PSTHGVYEHE VVAITSAVHD AGGQVYVDGA NLNALLGYAR FGDFGGDVSH LNLHKTFCIP
HGGGGPGVGP VAAKAHLAPF LPGHPLAQDD THVLATGGRV EHGGGPVSAA PYGSPSILPI
SWAYVRMMGA EGLRDATGAA VLAANYVAAR LREHFPVLYS GDAGLVAHEC ILDLRPLTER
TGVTVDDVAK RLVDYGFHAP TMSFPVAGTL MVEPTESEDL AELDRFVTAM IAIKAEADAV
AAGAWPVDDN PLRGAPHTAE SVVAADWSHP YTREQAVYPV PGLVRGKYWP PVRRIDQAYG
DRNLFCACPP PEAFS
//
