ID A3U2D2_PSEBH Unreviewed; 946 AA.
AC A3U2D2;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=OB2597_14851 {ECO:0000313|EMBL:EAQ01732.1};
OS Pseudooceanicola batsensis (strain ATCC BAA-863 / DSM 15984 / KCTC 12145 /
OS HTCC2597) (Oceanicola batsensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=252305 {ECO:0000313|EMBL:EAQ01732.1, ECO:0000313|Proteomes:UP000004318};
RN [1] {ECO:0000313|EMBL:EAQ01732.1, ECO:0000313|Proteomes:UP000004318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-863 / DSM 15984 / KCTC 12145 / HTCC2597
RC {ECO:0000313|Proteomes:UP000004318};
RX PubMed=20418400; DOI=10.1128/JB.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
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:EAQ01732.1}.
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DR EMBL; AAMO01000011; EAQ01732.1; -; Genomic_DNA.
DR RefSeq; WP_009807180.1; NZ_CH724131.1.
DR AlphaFoldDB; A3U2D2; -.
DR STRING; 252305.OB2597_14851; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_5; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000004318; 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:UP000004318}.
FT DOMAIN 16..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 617..727
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 765..885
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 698
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 946 AA; 102422 MW; 66CF3019E4A20B4C CRC64;
MTFTPTGYDA YDFANRRHIG PSPQEMEEML ATIGVNSLDE LIDRTVPRAI RQAEPLDFGA
PLSESELLSH MREVAGRNTV LTSLIGQGYH NTITPPAIKR NIFENPAWYT AYTPYQPEIS
QGRLEALLNY QTMVCDLTGL DIANASLLDE STAAAEAMTM AQRASKSKSM KFFVDEACHP
QNIDVIRTRA EPLGIEVVLG RPSDLVADEV FGAIFQYPGT NGVLRDFTPQ MEALHAAKAI
GIVIADPMAL CLLKEPGAMG ADIAVGSTQR FGVPLGYGGP HAAYMACKDA LKRSMPGRIV
GVSIDARGNR AYRLSLQTRE QHIRREKATS NVCTAQALLA VMASMYAVFH GPSGLKAIAQ
GIHARTVTMA RGLRDAGFDV FPKKVFDTVT VEVGPFQGAI LKSAVEEGLN LRRVGTTRIG
ITLDEVTTPD TIAAVWRAFG ITGPVPESTT YDLPEKLVRE TPYLTHEIFH MNRAETEMMR
YMRRLADRDL ALDRAMIPLG SCTMKLNAAA EMIPVSWDEI SSLHPFVPAD QAEGYTHLIA
DLSAKLCAIT GYNAFSMQPN SGAQGEYAGL LTIRNFHIAN GEGDRDVCLI PMSAHGTNPA
SAQMVGWKVV PIKSAANGDI DLQDFEAKAQ EHAGRLAAAM ITYPSTHGVF EETVTEVCKI
VHQHGGQVYI DGANLNAMVG LSRPGDLGGD VSHLNLHKTF CIPHGGGGPG MGPIGVKAHL
IPHLPGHTAQ GGTGAVSAAP FGSPSILPIS WAYCLMMGGE GLTQATRVAI LNANYIAARL
REAYPILYKG PLGHVAHECI LDTRPFAEVG VTVDDIAKRL MDCGFHAPTM SWPISGTLMV
EPTESETKAE LDRFCDAMLA IREEIMDIES GRHDHAASPL AHAPHTVEDL VGDWDRAYSR
EQGCFPPGAF RVDKYWPPVN RVDNVWGDRN LTCTCPPMSD YAVAAE
//
