ID B4RF15_PHEZH Unreviewed; 508 AA.
AC B4RF15;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
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:ACG77003.1};
GN OrderedLocusNames=PHZ_c0589 {ECO:0000313|EMBL:ACG77003.1};
OS Phenylobacterium zucineum (strain HLK1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG77003.1, ECO:0000313|Proteomes:UP000001868};
RN [1] {ECO:0000313|EMBL:ACG77003.1, ECO:0000313|Proteomes:UP000001868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG77003.1,
RC ECO:0000313|Proteomes:UP000001868};
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(2008).
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};
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DR EMBL; CP000747; ACG77003.1; -; Genomic_DNA.
DR RefSeq; WP_012521151.1; NC_011144.1.
DR AlphaFoldDB; B4RF15; -.
DR STRING; 450851.PHZ_c0589; -.
DR KEGG; pzu:PHZ_c0589; -.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_5_0_5; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000001868; Chromosome.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR CDD; cd00613; GDC-P; 1.
DR Gene3D; 6.20.440.10; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR049316; GDC-P_C.
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 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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001868}.
FT DOMAIN 180..299
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 372..470
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"
SQ SEQUENCE 508 AA; 53946 MW; 7BDD6498AC32CC36 CRC64;
MSMLNVGRPT RPEAAEPAQT SLTGGRGLLQ DEPLLFEVGG WDKTGVDLPD GPDADDLAGL
TRDGVDLPGL SEPEAVRHYV RLSQKNHAID LALYPLGSCT MKHNPRLNEK MARLAGFADL
HPLQPVSTTQ GALQLMDRLA HWLKTLTGMP AVALSPKAGA HGELCGLLCI KAAHEAAGQG
HRRTVLVPTS AHGTNPATAA FVGYSVTEIA QTDDGRVDLS DLAAKLGPDV AAIMVTNPNT
CGLFERDVIE IARLTHDAGA YFYCDGANFN AIVGKVRPGD LGVDAMHINL HKTFSTPHGG
GGPGAGPVVL SQALAPFAPA PWIVSGPDAL GLQEQDAGFG RMCAFHGQMG MFVRAYAYML
SHGADGLRQV AEDAVLNANY VKARLSDVMS PAFPEGPCMH EALFDDAWLD GTGVTTLDFA
KAMIDEGFHP MTMYFPLVVH GAMLIEPTET ESKAELDRFC EALRALAGAA KAGEAERFKG
APFLAPLRRL DETLAARKPK LAWTPPAE
//
