ID A0A0A1DPW0_NOCSI Unreviewed; 940 AA.
AC A0A0A1DPW0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=KR76_12865 {ECO:0000313|EMBL:AIY17425.1};
OS Nocardioides simplex (Arthrobacter simplex).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Pimelobacter.
OX NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY17425.1, ECO:0000313|Proteomes:UP000030300};
RN [1] {ECO:0000313|EMBL:AIY17425.1, ECO:0000313|Proteomes:UP000030300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY17425.1,
RC ECO:0000313|Proteomes:UP000030300};
RX PubMed=25573942;
RA Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT Ac-2033D.";
RL Genome Announc. 3:0-0(2015).
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:ARBA00043839, 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; CP009896; AIY17425.1; -; Genomic_DNA.
DR RefSeq; WP_038678781.1; NZ_JAAARG010000095.1.
DR AlphaFoldDB; A0A0A1DPW0; -.
DR STRING; 2045.KR76_12865; -.
DR KEGG; psim:KR76_12865; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_11; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000030300; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030300}.
FT DOMAIN 7..428
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 464..716
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 762..883
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 689
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 940 AA; 99583 MW; 0A6DD73024E2289D CRC64;
MSAPFVHRHI GPDDAQVETM LDRLGHPSLD ALMEAAVPKS IRATEALGLP DGVDEETAAA
ELRALAGANV PGEAMIGLGY HATVTPAVIR RNVLEDPSWY TAYTPYQPEI SQGRLEALIN
FQTMVADLTG LHTAGSSLLD EGTAAAEAVA LAFRANRKAS GPFVVDADAL PQTIDVVRTR
AEGIGIEVLV ADLSDGLPEG DVSGVLVQYP GASGRVPDIK PVIDAVHERG GLAVVAADLL
ALTLLEAPGT LGADVVVGSA QRFGVPLFYG GPHAGFISVR EGLERQLPGR LVGVSVDAEG
RPAYRLALQT REQHIRRDKA TSNICTAQVL LAVTAGMYAV YHGPQGLKDI AGDIHTLAGR
AAASLTGAGL ELVNDSFFDT LQVRVPGRAA DVVAAARAEQ LHLRLVDADT VGIAFGETAG
APTLRALHTA FGVTPAAAEP LAGLPEAQRR TTDFMTHPVF NTHHNETSML RYVTRLAHRD
YALDRGMIPL GSCTMKLNAT TEMEPISLAG FANLHPFVPA ADADGYRQLI EQLEGWLAEV
TGYDRVSVQP NAGAQGEFAG MLAIRNYHRA NGQDQRDVCL IPSSAHGTNP ASAVMAGMRV
VVVKAEDDGT VDLADLRAKC EQHADTLAAI MVTYPSTHGV YEETITELCD VVHEHGGQVY
IDGANFNALL GYAAPGRFGG DVSHLNLHKT FCIPHGGGGP GVGPVAVRAH LAPYLPTHPL
HPDAERRDGT GAISAAPFGS AGILPISWAY IRMMGGAGLT RATAVAVLSA NYVAARLGEH
FPVLYRGESG LVAHECILDL REITKETGVS VDDVAKRLVD YGFHAPTMSF PVAGTLMVEP
TESEDLAELD RFCDAMIAIK GEIDKVGAGE WAVDESPLHH APHTTRALVG EWDRAYSREV
AVFPAGHSVD KYWPPVARID QAYGDRNLVC ACPPIDAYSE
//
