ID A0A839T2N4_AZOMA Unreviewed; 953 AA.
AC A0A839T2N4;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
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=FHR87_001017 {ECO:0000313|EMBL:MBB3102634.1};
OS Azomonas macrocytogenes (Azotobacter macrocytogenes).
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pseudomonadales; Pseudomonadaceae; Azomonas.
OX NCBI_TaxID=69962 {ECO:0000313|EMBL:MBB3102634.1, ECO:0000313|Proteomes:UP000549250};
RN [1] {ECO:0000313|EMBL:MBB3102634.1, ECO:0000313|Proteomes:UP000549250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 4462 {ECO:0000313|EMBL:MBB3102634.1,
RC ECO:0000313|Proteomes:UP000549250};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) 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=N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein]
CC + glycine + H(+) = N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; 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:ARBA00049026, 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:MBB3102634.1}.
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DR EMBL; JACHXI010000003; MBB3102634.1; -; Genomic_DNA.
DR RefSeq; WP_183165616.1; NZ_JACHXI010000003.1.
DR AlphaFoldDB; A0A839T2N4; -.
DR Proteomes; UP000549250; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:TreeGrafter.
DR GO; GO:0016594; F:glycine binding; IEA:TreeGrafter.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR CDD; cd00613; GDC-P; 2.
DR FunFam; 3.40.640.10:FF:000005; Glycine dehydrogenase (decarboxylating), mitochondrial; 1.
DR FunFam; 3.40.640.10:FF:000007; glycine dehydrogenase (Decarboxylating), mitochondrial; 1.
DR FunFam; 3.90.1150.10:FF:000007; Glycine dehydrogenase (decarboxylating), mitochondrial; 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); 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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 NCBIfam; NF003346; PRK04366.1; 1.
DR PANTHER; PTHR11773:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 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.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00711}; Reference proteome {ECO:0000313|Proteomes:UP000549250}.
FT DOMAIN 18..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 460..729
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 779..900
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 707
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 953 AA; 103881 MW; A1BDE7E643D08EE6 CRC64;
MSHSSRLSQL HQADAFLDRH LGPDKAEQHA LLDALGLANR AQLIEQTVPP AIRLRGELEL
PAALDEQEAL ARLREHAMRN QQWTSLIGTG YHGTITPPVV LRNVLENPGW YTAYTPYQPE
IAQGRLEALL NFQQLTIDLT GLDLANASLL DEATAAAEAM ALARRVAKNK SNRFFVDENC
HPQTISVVRT RAEAFGFELV VDALDNLGAH DVFGALLQYP DTHGDIRDLR PLIEQLHTRQ
ALACVAADLL SLLLLMSPGE LGADVALGST QRFGVPMGFG GPHAAYFATR DEFKRAMPGR
IIGVSKDTRG NTALRMALQT REQHIRREKA NSNICTSQVL LANIAGFYAV YHGPEGLKRI
AERVYRLTSI LAAALERKGI QRINQYFFDT LTLDVGGAQT AIIESAKAAR INLRILGRGR
LGVSLDETCT RQTVEQLLSI FLGADHGLEI DLLDASELPQ GVPAELVRRS AYLTHPVFNT
HHSETEMLRY LKRLENKDLA LNQAMIPLGS CTMKLNATSE MIPITWPEFA NLHPFVPSEQ
AVGYRAMIDE LESWLCAITG FDAISMQPNS GAQGEYAGLL AIRKYHESRG EAQRDICLIP
ASAHGTNPAS AQMTSMRVVT VDCDKSGNVD LDDLKRKAAQ AGGQLACLMI TYPSTHGVYE
EGIRDICTVV HEQGGQVYMD GANLNALVGL ARPADVGADV SHMNLHKTFC IPHGGGGPGM
GPIGVKAHLA PFVANHPVVE LEGPAPGNSA VSAAPWGSAS ILPISWMYIA MMGPRLRDAT
EVAILNANYL ANRLNGAFPV LYSGRNGRVA HECIIDLRPL KAQTGISEED VAKRLMDYGF
HAPTMSFPVP GTLMIEPTES EPKAELDRFV EAMLSIRAEI AKVQNGEWTA EDNPLVNAPH
TLADVTGAWT RAYSIAEAVT PSAHTREHKY WPTVNRVDNV FGDRNLFCAC VSG
//
