ID A0A1A0NCF8_9MYCO Unreviewed; 946 AA.
AC A0A1A0NCF8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=A5662_18825 {ECO:0000313|EMBL:OBA95282.1};
OS Mycobacteriaceae bacterium 1482268.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae.
OX NCBI_TaxID=1834080 {ECO:0000313|EMBL:OBA95282.1, ECO:0000313|Proteomes:UP000091934};
RN [1] {ECO:0000313|EMBL:OBA95282.1, ECO:0000313|Proteomes:UP000091934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1482268.1 {ECO:0000313|EMBL:OBA95282.1,
RC ECO:0000313|Proteomes:UP000091934};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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:OBA95282.1}.
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DR EMBL; LZSH01000347; OBA95282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A0NCF8; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000091934; 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; 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 {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}.
FT DOMAIN 9..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 470..725
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 767..888
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 697
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 946 AA; 100573 MW; 5ABB20B68C746DF4 CRC64;
MPESPTFADR HIGPDADAVA TILKTIGVGS LDELADKALP AGILDALCAD GIAPGLDQLP
HAATEDQALA ELRALADANT VAVSMIGQGY YDTLTPPVLR RNILENPAWY TAYTPYQPEI
SQGRLEALLN FQTMVADLTG LEVANASMLD EGTAAAEAMT LMHRAVRGTS NRLAVDSDLF
SQTAAVLATR AEPLGIEIVT ADLRGGLPDG EFFGVITQLP GAGGELVDWT ALVNQAHERG
ALVAIGADLL ALTLIAPPGD IGADVAFGST QRFGVPMGFG GPHAGYLAVH TNHARQLPGR
LVGVSVDADG SPAYRLSLQT REQHIRRDKA TSNICTAQVL LAVIAAMYAS YHGADGLTGI
ARRVHHRARA LAAGLSAAGV EVVHDRFFDT VLARVPGRAA EVRDKAKSRG INVWLVDDDH
VSVSCDEATG QEHIDNVLAA FGAPTGAGDF DGPALATRTS EFLTHPAFTR YRTETEMMRY
LRSLADKDIA LDRSMIPLGS CTMKLNAAAE MEPITWPEFA RQHPFAPHSD APGLRKLIAD
LESWLAQLTG YDAVSLQPNA GSQGEYAGLL AIQAYHAERG ERDRNVCLIP SSAHGTNAAS
AALAGMRVVV VACRANGDVD LDDLRAKVAE HADRLSALMI TYPSTHGVYE HDIADICAAV
HDVGGQVYVD GANLNALVGL ARPGKFGGDV SHLNLHKTFC IPHGGGGPGV GPVAVRAHLR
PYLPGHPLAE ELPDEHTVSS APYGSASILP ITWAYIRMMG AQGLRAASLT AIASANYIAR
RLDEYYPVLY TGENGMVAHE CILDLRGITK STGVTVDDVA KRLADYGFHA PTMSFPVAGT
LMVEPTESES LAEVDAFCEA MIAIRAEIDQ VGSGAWPADD NPLRGAPHTA ESLLVDEWSH
PYTREQAAYP LGKHFRPKVW PPVRRIDSAY GDRNLMCSCP PVEAFA
//
