ID D0JBS5_BLASB Unreviewed; 957 AA.
AC D0JBS5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN Name=gcvP {ECO:0000313|EMBL:ACY40613.1};
GN OrderedLocusNames=BLBBGE_616 {ECO:0000313|EMBL:ACY40613.1};
OS Blattabacterium sp. subsp. Blattella germanica (strain Bge) (Blattella
OS germanica symbiotic bacterium).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=331104 {ECO:0000313|EMBL:ACY40613.1, ECO:0000313|Proteomes:UP000002625};
RN [1] {ECO:0000313|EMBL:ACY40613.1, ECO:0000313|Proteomes:UP000002625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bge {ECO:0000313|Proteomes:UP000002625};
RX PubMed=19911043; DOI=10.1371/journal.pgen.1000721;
RA Lopez-Sanchez M.J., Neef A., Pereto J., Patino-Navarrete R., Pignatelli M.,
RA Latorre A., Moya A.;
RT "Evolutionary convergence and nitrogen metabolism in Blattabacterium strain
RT Bge, primary endosymbiont of the cockroach Blattella germanica.";
RL PLoS Genet. 5:E1000721-E1000721(2009).
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}.
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};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC 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}.
CC -!- SIMILARITY: Belongs to the GcvP family.
CC {ECO:0000256|ARBA:ARBA00010756}.
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DR EMBL; CP001487; ACY40613.1; -; Genomic_DNA.
DR RefSeq; WP_012841128.1; NC_013454.1.
DR AlphaFoldDB; D0JBS5; -.
DR STRING; 331104.BLBBGE_616; -.
DR KEGG; bbl:BLBBGE_616; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_10; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000002625; Chromosome.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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 InterPro; IPR000192; Aminotrans_V_dom.
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; PF00266; Aminotran_5; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR Pfam; PF02347; GDC-P; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACY40613.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50}.
FT DOMAIN 14..447
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 587..720
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 786..905
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 714
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 957 AA; 109985 MW; A0A1315A8274672D CRC64;
MKEDYIRRKK FYYRHIGPSC NEINDMLKEL QCSSIKNFIK KTIPKEIRLK RKLNLPNSIS
EYQYLNHIYK ISKKNKIYRS YIGLGYKNTI TPSVIQRNIL ENPSWYTPYT PYQSEISQGR
LEALINFQTM ISDLTGMKIS NASMLDESTA SADAMFMIYQ EKIKKKQIDN HYCFFVSDEI
LPQTFSVLKT RCFGLGIQII IDTHKNLLKG KYNGKKIFGL MISYPTCLGE IYDYSETIEY
DKKNNISVIV SADILSLSLL KPPGEWGADV VVGSSQSFGV PMGYGGPHAA FFSTHEKYKR
FIPGRIIGIS IDNKNKKAYR MALQTREQHI KRERATSNIC TSQVLPAIMA SMYALFHGKE
GLIGIAKSIH EYAKKLEFLL INSINNLSQV NTFYFDTIRI KTDFIDQLKE VSDRKKTNFR
YIDKNHLTIT LDETTCEKDI DHILSIFHEV YKKRKKFDDT NQIHKKYKFP SSLKRTSNFL
EHEIFHKFYS ENELMRYIKR LERKDLSLIH SMIPLGSCTM KLNASTELFS LSQHEWRNVH
PFAPDKQTMG YRLVIRNLKK YLKEITGFSG ISLQPNSGAQ GEYAGLMVIK SYHHSLQETK
RNIALIPSSS HGTNPASANM AGMKVILIST KNDGSIDRND LFKKVKEYKD FLSVLMITYP
STYGVYETHI QEIINMIHEN GGQVYMDGAN MNAQVGLIKP AHLGVDVCHL NLHKTFAIPH
GGGGPGMGPI CVASHLKPFL PDHPFFGKLE KNKLTISSSP YGSSLILTIS YAYIRLLGPD
GLRKCTEISI LNANYIKEKL KKFYNTLYVG KNNAVAHELI IDCRIFKSLD IEVIDIAKRM
MDYGYHAPTV SFPVEGCMMI EPTESESKEE LDRFIETLIN IRKEIQEIED GKFSKKENVL
KNAPHSIELL TDNDWNYPYS REKAAYPLYW VRERKFWPSV NRIDDGYGDR NLMCTCN
//
