ID A0A257ISI3_9BACT Unreviewed; 956 AA.
AC A0A257ISI3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:OYU65609.1};
GN ORFNames=CFE22_13205 {ECO:0000313|EMBL:OYU65609.1};
OS Cytophagaceae bacterium BCCC1.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae.
OX NCBI_TaxID=2015573 {ECO:0000313|EMBL:OYU65609.1, ECO:0000313|Proteomes:UP000215757};
RN [1] {ECO:0000313|EMBL:OYU65609.1, ECO:0000313|Proteomes:UP000215757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCCC1 {ECO:0000313|EMBL:OYU65609.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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:OYU65609.1}.
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DR EMBL; NKJF01000032; OYU65609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257ISI3; -.
DR Proteomes; UP000215757; 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:UP000215757}.
FT DOMAIN 13..440
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 457..736
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 777..898
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 705
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 956 AA; 105147 MW; 03D640C64E8821EF CRC64;
MKVTLTNHEK FEKRHQGKTS SELESMCIEI GVENLEQLID ETVPANIRLD KMLNLPAALS
ETQLLEKLKF LGSKNKVYKS FIGGGYYDTA VPKVILRNIL ENPSWYTAYT PYQAEIAQGR
LEMLLNFQTI VTDLTGMEIS NASLLDEATA AAEAMSMFYN IKKGAKKNAN DFFISESCHP
QVIDVITGRA TPIGVNIIVG NQDTFDFEKS NVFGAMFQNP NTFGEITDYT DLISRLHTSD
IKVCVGIDLL SLTIFKNPGQ MGADVVIGTS QRLGVPMGYG GPHAAFFATK DEFKRHIPGR
IIGKSIDSEG NPALRMALQT REQHIRREKA TSNICTAQVL LSVMSAAYCI YHGPDGLKEI
ALKIHGLTKS FANAVQGLDY RVLNQNYFDT ITLDVLDNTK IRQIAESRGV NFRYHGTEDI
SISFDETKTL EDLGLLLEIF AEARGESLVM NLKHDVEISI PENLGREDDY MKHPVFNSYH
TEHEMLRYLK SLESKDLSLV HSMISLGSCT MKLNATSEMI AVTWPEFGNI HPFAPVDQTV
GYQMMFDELC DWLSEITGFA KVSLQPNSGA QGELAGLMVI RAFHEQNNHG ARNIALIPSS
AHGTNPASAV MAGMKVVVVK CDEKGNIDVE DLKLKAAEHA EDLACLMVTY PSTHGVFEET
IIEICEIIHS YGGKVYMDGA NMNAQVGLTS PGKIGADVCH LNLHKTFAIP HGGGGPGVGP
IGVTAELATF LPGNAVIKTG GEKAINGISA APWGSASVLP ISYAYIAMMG PDGLTNATKY
AILNANYIKS RLEKHFDILY TGSNGHCAHE MIVECRPFKM SAHVEVEDIA KRLMDYGFHA
PTVSFPVAGT LMIEPTESES KAELDKFCDA LIAIREEIAE IESGIYPADN NVLVNAPHTQ
RVVMVENWDK SYSREKAAFP NEKLKFNKFW PAVSRIDSAY GDRNLVCACE PIEAYA
//
