ID D5RSU6_9PROT Unreviewed; 966 AA.
AC D5RSU6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
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:EFH09620.1};
GN ORFNames=HMPREF0731_4158 {ECO:0000313|EMBL:EFH09620.1};
OS Pseudoroseomonas cervicalis ATCC 49957.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=525371 {ECO:0000313|EMBL:EFH09620.1, ECO:0000313|Proteomes:UP000005324};
RN [1] {ECO:0000313|EMBL:EFH09620.1, ECO:0000313|Proteomes:UP000005324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49957 {ECO:0000313|EMBL:EFH09620.1,
RC ECO:0000313|Proteomes:UP000005324};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (APR-2010) 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:EFH09620.1}.
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DR EMBL; ADVL01000759; EFH09620.1; -; Genomic_DNA.
DR RefSeq; WP_007003188.1; NZ_GG770777.1.
DR AlphaFoldDB; D5RSU6; -.
DR HOGENOM; CLU_004620_3_2_5; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000005324; 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:UP000005324}.
FT DOMAIN 20..446
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 486..737
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 783..904
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 710
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 966 AA; 102101 MW; 6501FB7E45A601DF CRC64;
MSDALHELAA LEDHGAFAAR HIGPSEAEIA AMLQAVGAAS LDDLADRTVP AAIRGQDFSQ
LPPPVSEAEA IAELRALSEL NTRRRSLIGM GYHGTHVPPV ILRNVLENPG WYTAYTPYQA
EIAQGRLEAL VNFQTMVCDL TGLPVANASL LDEATAAAEA MALALAASKS KSRTLLVAAD
VHPQTLAVIQ TRAEPLGLVV EVVPVSGISV AAAEKKPFAL VLQYPGTTGE VRDIAPEIAA
VQAVGGLAIV ASDPLSLVLL TPPGEMGADV VIGSSQRFGV PMGYGGPHAA FMAVKDAYKR
LMPGRLVGVS VDAAGRPAMR LALQTREQHI RREKATSNIC TAQVLLAVMA GMYAVWHGPE
GLKRIARRVA LQARLLADAA VRAGFTLRHE AFFDTIAIEA GAKADALMAE ALSSGFNLRR
IDATGVGIAL DETVSRLELE TLLAVLGKVG GQAVALDALS PRGGLPAALA RRSAILTAQV
FNSHHAEHAM LRYLKSLEDK DVALNRSMIP LGSCTMKLNA TAEMIPVTFP GFGEMHPFVP
ADQAAGYIAM IRRLESWLAT ITGFAAVSLQ PNAGSQGEYA GLLAIRAWHK ARGEAQRDVC
LIPSSAHGTN PASAVMAGMR VVVVGCDRDG NVDLADLEAK IAQHADKLSA LMVTYPSTHG
VFEEEIIRIC DAVHAAGGQV YMDGANMNAQ VGLTAPGRIG ADVCHLNLHK TFCIPHGGGG
PGVGPIGVAA HLAPHLPNHP LLAEAGPATG YGPVSAAPFG SASILPISYA YIRMMGGAAL
TRATQVAILN ANYIAKRLDG HFPVLYKGAR GMVAHECILD CRGFQQGGGV LVEDIAKRLQ
DYGFHAPTMS WPVAGTLMVE PTESETKAEL DRFCDAMIAI RAEIRAVEQG RADRNDNPLK
NAPHTAAEVM SSDWAHPYSR EEAAFPLPFV AAHKYWPPVK RVDNVYGDRN LICTCAPLED
YAQAAE
//
