ID A0A222XB71_9CELL Unreviewed; 994 AA.
AC A0A222XB71;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=CBP52_14650 {ECO:0000313|EMBL:ASR56130.1};
OS Cellulomonas sp. PSBB021.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2003551 {ECO:0000313|EMBL:ASR56130.1, ECO:0000313|Proteomes:UP000214627};
RN [1] {ECO:0000313|EMBL:ASR56130.1, ECO:0000313|Proteomes:UP000214627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB021 {ECO:0000313|EMBL:ASR56130.1,
RC ECO:0000313|Proteomes:UP000214627};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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:ARBA00033655, 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}.
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DR EMBL; CP021430; ASR56130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222XB71; -.
DR KEGG; cez:CBP52_14650; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000214627; Chromosome.
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}.
FT DOMAIN 22..447
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 511..764
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 814..935
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 736
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 994 AA; 105355 MW; 13C43C4E16AC1CFA CRC64;
MSKTTPHSAP TGPAPAALDF SDRHVGPRRG AETDAMLAVV GYERIEDLID AAVPASIRTG
RPLALPEAQG EAEVQAALRE IAGRNQVLRP MIGQGYYGTT TPPVIRRNVL ESPAWYTAYT
PYQPEISQGR LEALLNFQTM VEDLTGLPVA NASLLDEATA VAEAVALMWR AQRGKAGTVV
LDDQLFGQSL AVTVGRAEAI GLPVVVADLS QGLPQVEGDL IGLVVQQVAA SGEVRDLRDV
IAATKERGGL VTVAADLLAL TLLTSPGTLG ADVAVGSAQR FGVPLFGGGP HAAFMAVRSG
LERMLPGRLV GVSVDADGAP AYRLALQTRE QHIRREKATS NICTAQALLA IVASMYAVHH
GPDGLRAIAS RVHGHAATLA ARLRDLGVEV EHEVVFDTVR TVVPGRAADV VAAGVRQGVN
LWAPDGDHVQ ASVDETTGDD DVLAVVLAFV AAGVTDAPSG GHDEQWTSPS GSFTVRGEAF
AYGPMAAPTA LPDWAVRTDE YLTHPVFHLY RSETAMLRYL RRLSDQDLAL DRTMIPLGSC
TMKLNATAEM EPISWPQFAD VHPYAPADQT QGYAELVTQL QDWLAEITGY AAVSVQPNGG
SQGEFAGLLA IKAYHRDRGE AQRDVCLIPA SAHGTNAASA ALAGLRVVVV ATAEDGEILL
DDLRAKLEEH GPRVAAIMIT YPSTHGVYEE HVRQVCDLVH DAGGQVYIDG ANLNALVGLA
RPGEMGGDVS HLNLHKTFCI PHGGGGPGVG PVAVAAHLAP YLPGDPTTSP RTPDAAAHAS
HVPAVSAAPW GSAGILPISW AYVALMGPDG LRRATEVAVL AANYLATRLR EHFPVLYTGP
NGLVAHECIL DLREITRRTG VTAEDVAKRL MDYGFHAPTL AFPVPGTLMV EPTESEDLAE
LDRFVDAMVA IRAEIDEVAA GTWPLEDSPL RHAPHTAQSV SADGWTHAYS RERAAFPLAS
LRRGKYWPPV RRIDGARGDR NLVCSCPPVE AFAE
//