ID A0A367AF10_9ACTN Unreviewed; 993 AA.
AC A0A367AF10;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ECO:0000313|EMBL:RBY87928.1};
GN ORFNames=DQ241_09910 {ECO:0000313|EMBL:RBY87928.1};
OS Blastococcus sp. TF02A-30.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=2250580 {ECO:0000313|EMBL:RBY87928.1, ECO:0000313|Proteomes:UP000253175};
RN [1] {ECO:0000313|EMBL:RBY87928.1, ECO:0000313|Proteomes:UP000253175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02A-30 {ECO:0000313|EMBL:RBY87928.1,
RC ECO:0000313|Proteomes:UP000253175};
RA Ennis N., Dharumadurai D., Sevigny J., Morris K., Simpson S., Thomas W.K.,
RA Tisa L.S.;
RT "Genome Sequence of Blastococcus sp. TF02-30.";
RL Submitted (JUL-2018) 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: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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBY87928.1}.
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DR EMBL; QOHJ01000004; RBY87928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367AF10; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000253175; Unassembled WGS sequence.
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:UP000253175}.
FT DOMAIN 20..447
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 463..736
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 778..899
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 708
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 993 AA; 104513 MW; AD0DB9A1FCA27D03 CRC64;
MTDGLPSLSD LQPAGSFAGR HIGPRPADTA AMLEAVGFDS LAALADAAVP EGVRDRSPLR
LPAAADEAAV LAELRERAAD NEVFTSMIGL GYSGTITPPV IQRMVLENPA WYTAYTPYQP
EISQGRLEAL INFQTMVADL TGLDVAGASM LDEATAAAEA MTLVRRAGRA RPDAVFVVDA
DTLPQTLAVL ETRAEPLGIR LHVADLSAGW PTDLPEAGAF GVLLSFPGAS GAVRDHRALA
AAAHEAGAQV VVAADLLALT LLEAPGEWGA DVACGTTQRF GVPLGYGGPH AGYLSVREGL
ARQLPGRLVG VSVDADGDVA YRLALQTREQ HIRREKATSN ICTAQVLLAV MAGAYAVYHG
PEGLAVIAAR VHRSAQTLAN WLADGGLELA HPAYFDTLQV RVPGRADDVL AAAAQRRINL
RRVDADTVAV ACDETTTPEI LRAVAEAFGV AAGEPAGDGA DALPAELRRR TAYLTHPVFS
AHRSETAMLR YLRALSDKDL ALDRTMIPLG SCTMKLNAAT EMAAITWPEF ANLHPFAPAE
QARGYARLID ELCTWLAEVT GYAAVSVQPN AGSQGEFAGL MAIRGYHRSR GDDQRDVCLI
PSSAHGTNAA SAVMAGMRVV VVACDEAGNV DVADLRAKVD QHAERLAAIM LTYPSTHGVF
EVDVQEICAA VHDAGGQVYV DGANLNAMVG LARPGRFGSD VSHLNLHKTF CIPHGGGGPG
VGPIGVAEHL VPFLPGHPLA DTGGRGPAIS GAPWGSAGIL PISWAYVRLM GPDGLLAATE
HAILAANYLA TRLREHFPVL YTGAGGLVAH ECILDIRPLT KATGVTNDDI AKRLIDFGFH
APTMSFPVAG TLMVEPTESE DRGELDRFVE AMVTIRGEIE KVATGEYDRA DNPLRNAPHT
LAMLAGEWGR PYQRTTAVYP VRGLQGRSYL SPVRRIDQAY GDRNLVCACP PPEAFAEHDF
GDHAPSVNGS TPSRAGGAPD DLGTAGDVVA AGR
//
