ID A0A2A2G910_9BACT Unreviewed; 971 AA.
AC A0A2A2G910;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:PAU93494.1};
GN ORFNames=CK503_12240 {ECO:0000313|EMBL:PAU93494.1};
OS Aliifodinibius salipaludis.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX NCBI_TaxID=2032627 {ECO:0000313|EMBL:PAU93494.1, ECO:0000313|Proteomes:UP000218831};
RN [1] {ECO:0000313|EMBL:PAU93494.1, ECO:0000313|Proteomes:UP000218831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN023 {ECO:0000313|EMBL:PAU93494.1,
RC ECO:0000313|Proteomes:UP000218831};
RA Liu D., Zhang G.;
RT "Aliifodinibius alkalisoli sp. nov., isolated from saline alkaline soil.";
RL Submitted (AUG-2017) 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:PAU93494.1}.
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DR EMBL; NSKE01000008; PAU93494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2G910; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000218831; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000218831}.
FT DOMAIN 12..443
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 461..742
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 784..904
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 711
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 971 AA; 108170 MW; B4D929171C4F0136 CRC64;
MSINFDKERF MHRHNGPDEK QESEMLSAID ASSIDELIDQ TIPKGIRLQD QIDLDEPMSE
YRFLEEFRKL ANKNEIFDSY IGMGYHDTLT PNVILRNVLE NPGWYTAYTP YQAEIAQGRL
EALINFQTMV SDLTGRELAN ASLLDEGTSA AEAMSMLYSM RRGAKRKKAH KFFVSELCHP
QTIDVIEGRA EPLDIEVVVG DHHDLDVTDE ELFGMLLQYP ATDGTVEDYS DLIAACEENN
VQSVVAADLL SLTLLTPPGE MGADVVVGST QRFGVPMGYG GPHAAYFATR EKYKRKIPGR
IIGVTQDTEE NPVYRMALQT REQHIRREKA TSNICTAQVL LAVIAGFYAV YHGPKGLRRI
AERIHGLAKV MDKGLEKLGF EVANDLYFDT LKVKLEDDNQ KEKLRQKALN HKLNLRYFDE
PAVGIAFDEV KDLDHVEELL AIFASLNDKG DKVNVAELSK SVEIDYPEGL TRTSDYLEHP
VFNLYHSEHE MLRYLKKLEN KDLSLVHSMI SLGSCTMKLN ATSEMIPLTW PEFGKLHPFA
PQGQAEGYHE LFDKLEHQLA AITGFPAVSL QPNSGAQGEF SGLMTIRAYH KHHGEEHRNV
TIVPDSAHGT NPASAVMAGM DVVVTKCDEH GNIDLDDLRE KVEANKENLA ALMVTYPSTH
GVFEEDIKEI CQVIHDNGGL VYMDGANMNA QVGLTSPAEI GADVCHLNLH KTFCIPHGGG
GPGMGPIAAT KDLAPFLPGN PVKDTGGEHA IKSISAAPWG SASILSISYA YIKMMGAEGL
TKVSETAILN ANYLKEQLKD HYPILYTGKN GRTAHEFIVD IRPFKQSAGI ESIDVAKRLM
DYGFHAPTMS FPVPGTLMVE PTESETKEEL DRFCEAMISI REEIKEIEEG NADPENNVLK
HAPHTMRVAM AEDWDQPYSR EKAIFPLDYL RFNKFWPAVS RVDDAYGDRN LMCNCVPIDA
YSEGQEPTAV D
//
