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Database: UniProt
Entry: A0A222XB71_9CELL
LinkDB: A0A222XB71_9CELL
Original site: A0A222XB71_9CELL 
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
//
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