ID GCSP_BORA1 Reviewed; 955 AA.
AC Q2KYL7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711}; OrderedLocusNames=BAV0493;
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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:0000255|HAMAP-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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00711};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP-
CC Rule:MF_00711}.
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DR EMBL; AM167904; CAJ48098.1; -; Genomic_DNA.
DR RefSeq; WP_012416189.1; NC_010645.1.
DR AlphaFoldDB; Q2KYL7; -.
DR SMR; Q2KYL7; -.
DR STRING; 360910.BAV0493; -.
DR GeneID; 41392404; -.
DR KEGG; bav:BAV0493; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_2_1_4; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000001977; 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; 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; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..955
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_1000045566"
FT MOD_RES 702
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 955 AA; 102819 MW; 93E0C5A398CC62FD CRC64;
MSRALDTHSD FIPRHIGPSE ADQAKMLATI GCSSLDALLE EVVPPRIRNQ APLALPGARS
EPDVLAELKQ MAARNKVFRN YIGQGYYGTH TPNVVLRNVL ENPAWYTAYT PYQPEISQGR
LEALLNYQTM VADLTGLDIS NASLLDEGTA AAEAMTLARR SAKSKSAVFF VSQHCHPQTI
EVVRTRAQGL DIDVLVGDES QGLPECFGVL LQYPHSLGGV VNYRELAEAA HAQGAVVACA
TDLLALALLT PPGEWGADIA VGTAQRFGVP FGFGGPHAGF MACRDAFKRN MPGRLVGVSK
DAQGNPALRL ALQTREQHIR REKATSNICT AQVLLAVMAG LYAVWHGPAG LRRIATRVHT
FAGVLRQHVQ ALGLTVENDS YFDTLLINTG PATPAVLRAA ECAHINLRRV DAGRVAVSID
ETVTVEDLQA LINVFAAGLG KDDITLDAAT LAPEAGLPAG TVRTSPILSH PVFSSVQSET
DMLRYLRKLA DKDLALDRSM IPLGSCTMKL NATAEMIPIT WPEFALIHPF APADQTAGYR
ELIERLSAAL CEITGYDNIS LQPNSGAQGE YAGLLAIRGY HQARGEHQRN ICLIPSSAHG
TNPASAQLAG MDVVVVASDD HGNVDLDDLR AKIEQVGDRL AALMITYPST HGVFEETVTE
ICERVHAAGG QVYLDGANMN AMVGVAKPGK FGSDVSHLNL HKTFCIPHGG GGPGVGPVAV
RAHLAPYLPG VLNEQGKLDA EAKVGPVSAA PYGSAGILAI PFVYISLMGA EGLRRATEVA
ILNANYVATR LREYYPVLYA GRHGRVAHEC ILDIRPLKES IGISAEDIAK RLMDYGFHAP
TMSFPVAGTL MVEPTESEGL AELERFIDAM IAIRAEVAQV ERGERDREDN VLKNAPHTAQ
MLLAEEWHHA YPRQQAAYPL ASLRDGKYWP PVARVDNAYG DRNLVCSCLP IEAYI
//
